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Waggle dance
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This article is about bee behavior. For the beer, see Wells & Young's Brewery. For the football play, see bootleg play.
The waggle dance - the direction the bee moves in relation to the hive indicates direction; if it moves vertically the direction to the source is directly towards the Sun. The duration of the waggle part of the dance signifies the distance.
Waggle dance is a term used in beekeeping and ethology for a particular figure-eight dance of the honey bee. By performing this dance, successful foragers can share, with other members of the colony, information about the direction and distance to patches of flowers yielding nectar and pollen, to water sources, or to new nest-site locations.[1][2] The waggle dance and the round dance are two forms of dance behaviour that are part of a continuous transition. The round dance occurs for resources that are nearby (typically less than 10–20 m from the nest for Apis mellifera ligustica). As the distance to the resource increases, the round dance transforms into the waggle dance. However, even close to the nest, the round dance can contain elements of the waggle dance, such as a waggle portion.[3] It has therefore been suggested that the term "waggle dance" is better for describing both the waggle dance and the round dance.[4] Austrian ethologist and Nobel laureate Karl von Frisch was one of the first who translated the meaning of the waggle dance.[5]
Contents
[hide]
1 Description
2 Mechanism
3 Controversy
3.1 The dance language vs. the waggle dance
3.2 Dance language as a language
3.3 Efficiency and adaptation
4 Evolution
5 Applications to operations research
6 See also
7 References
7.1 Further reading
8 External links
Description[edit]
Figure-eight-shaped waggle dance of the honeybee (Apis mellifera). A waggle run oriented 45° to the right of ‘up’ on the vertical comb (A) indicates a food source 45° to the right of the direction of the sun outside the hive (B). The abdomen of the dancer appears blurred because of the rapid motion from side to side.
A waggle dance consists of one to 100 or more circuits, each of which consists of two phases: the waggle phase and the return phase. A worker bee's waggle dance involves running through a small figure-eight pattern: a waggle run (aka waggle phase) followed by a turn to the right to circle back to the starting point (aka return phase), another waggle run, followed by a turn and circle to the left, and so on in a regular alternation between right and left turns after waggle runs. Waggle-dancing bees produce and release two alkanes, tricosane and pentacosane, and two alkenes, (Z)-9-tricosene and (Z)-9-pentacosene, onto their abdomens and into the air.[6]
The direction and duration of waggle runs are closely correlated with the direction and distance of the resource being advertised by the dancing bee. The resource can include the location of a food source or a potential nesting site.[7] For cavity-nesting honey bees, like Apis mellifera or Apis nigrocincta, flowers that are located directly in line with the sun are represented by waggle runs in an upward direction on the vertical combs, and any angle to the right or left of the sun is coded by a corresponding angle to the right or left of the upward direction. The distance between hive and recruitment target is encoded in the duration of the waggle runs.[1][8] The farther the target, the longer the waggle phase. The more excited the bee is about the location, the more rapidly it will waggle, so it will grab the attention of the observing bees, and try to convince them. If multiple bees are doing the waggle dance, it's a competition to convince the observing bees to follow their lead, and competing bees may even disrupt other bees' dances or fight each other off. In addition, some open-air nesting honeybees, like Apis andreniformis, whose nests hang from twigs or branches, will perform a horizontal dance on a stage above their nest in order to signal to resources.[9]
Waggle dancing bees that have been in the nest for an extended time adjust the angles of their dances to accommodate the changing direction of the sun. Therefore, bees that follow the waggle run of the dance are still correctly led to the food source even though its angle relative to the sun has changed.
The consumption of ethanol by foraging bees has been shown to reduce waggle dance activity and increase occurrence of the tremble dance.[10]
Kevin Abbott and Reuven Dukas of McMaster University in Hamilton, Ontario, Canada discovered that if a dead Apis mellifera bee is placed on a flower, bees performed far fewer waggle dances upon returning to the hive. The scientists explain that the bees associate the dead bee with the presence of a predator at the food source. The reduction of the dance repetition frequency, therefore, indicates that the dancing bees perform and communicate a form of risk/benefit analysis.[11][12]
Though first decoded by Karl von Frisch, dancing behavior in bees had been observed and described multiple times prior. Around 100 years before Frisch's discovery, Nicholas Unhoch described dancing behavior of bees as being an indulgence "in certain pleasures and jollity".[5] He did, however, admit ignorance as to the purpose of the dancing. 35 years prior to Unhoch's observations, Ernst Spitzner observed bees dancing and interpreted it as transmitting forage resource odors to other nestmates.[5] Even Aristotle, in addition to describing flower constancy behavior, suspected that some form of communication occurred between foragers within a nest:
"On each trip the bee does not fly from a flower of one kind to a flower of another, but flies from one violet, say, to another violet, and never meddles with another flower until it has got back to the hive; on reaching the hive they throw off their load, and each bee on her return is followed by three or four companions. What it is that they gather is hard to see, and how they do it has not been observed".[13]
Jürgen Tautz also writes about it in his book "The Buzz about Bees":
Page 112: Many elements of the communication used to recruit miniswarms to feeding sites are also observed in "true" swarming behavior. Miniswarms of foragers are not placed under the same selection pressure as are true swarms, because the fate of the entire colony is not at stake. A truly swarming colony has to be quickly led to a new home, or it will perish. The behavior used to recruit to food sources possibly developed from the "true" swarming behavior.
Tautz, J.: The Buzz about Bees - Biology of a Superorganism (photos by H. R. Heilmann) Springer Heidelberg & Berlin, 2008
Mechanism[edit]
Honeybees accumulate an electric charge during flying and when their body parts are moved or rubbed together. Bees emit constant and modulated electric fields during the waggle dance. Both low- and high-frequency components emitted by dancing bees induce passive antennal movements in stationary bees according to Coulomb's Law. The electrically charged flagellum of mechanoreceptor cells are moved by electric fields and more strongly so if sound and electric fields interact. Recordings from axons of the Johnston's organ indicate its sensitivity to electric fields. Therefore, it has been suggested that electric fields emanating from the surface charge of bees stimulate mechanoreceptors and may play a role in social communication during the waggle dance.[14]
Controversy[edit]
Workers of Apis mellifera carnica on honeycomb
The dance language vs. the waggle dance[edit]
As defined by von Frisch, Tanzsprache (German for "dance language") is the information about direction, distance, and quality of a resource (such as food or nesting sites) contained within the waggle dance.[15] There is supporting evidence of the waggle dance and "Tanzsprache" in Apis dorsata. Similar to other bees, they utilize the dance language to indicate the critical information regarding food resources. The dancer's body points in the direction of the food source and the sound produced during the dance indicates the profitability of the food.[16] Although there is some evidence for a direct connection between the Tanzsprache and the performance of the waggle dance, recent criticism holds that potential foragers need not correctly translate the dance language from the waggle dance to successfully forage.[15] In an experiment on the honeybee Apis mellifera, most individuals who thoroughly followed a waggle dance ignored the resource direction and location information. Instead, 93% of the foragers returned to foraging areas they had previous knowledge of.[15]
Bees that follow a waggle dance can successfully forage without decoding the dance language information in several ways:[17]
Dance follower may use olfactory information from the dancer and find either the same resource or a different one with a similar scent.
Following a dance may simply trigger foraging behavior. A forager may then search randomly for resources.
Following a dance may reactivate private knowledge of a resource. After reactivation, the forager may return to the known resource.
Using information communicated in the waggle dance is more useful to foragers when private information about resources is lacking.
Dance language as a language[edit]
The use of the word "language" may lead to misrepresentations of the waggle dance. The Swiss linguist Ferdinand de Saussure proposed a system of language where a sign is made up two chief components. The signifier is the physical or phonetic representation of a sign. The signified is the conceptual component.[18] If the dance language followed the Saussurian dyadic model of semiotics, the signifier would be the waggle dance and the signified would be the location of the foraging resource. Though the dance language may or may not follow this sort of pattern, it is not considered to be a language with syntactical grammar or a set of symbols.[17]
Efficiency and adaptation[edit]
The waggle dance may be less efficient than once thought. Some bees observe over 50 waggle runs without successfully foraging, while others will forage successfully after observing 5 runs.[17] Likewise, studies have found that honeybees rarely make use of the information communicated in the waggle dance and seem to only do so about ten percent of the time.[19][20] Evidently there is a conflict between private information, or individual experience, and social information transmitted through dance communication. This sheds light on the fact that following social information is more energetically costly than foraging independently and is not always advantageous.[21][22] Using olfactory cues and memory of plentiful foraging sites, honeybees are able to successfully forage independently without expending the potentially extensive energy it takes to process and execute the directions communicated by their fellow foragers.
The waggle dance may be adaptive in some environments and not in others, which provides a plausible explanation as to why the information provided by waggle dances are only used sparingly. Depending on weather, other competitors, and food source characteristics, transmitted information may become obsolete quickly.[23] As a result, foragers reported to be attached to their food sites and continue to revisit a single patch many times after it has become unprofitable.[24] For example, the waggle dance plays a significantly larger role in foraging when food sources are not as abundant.[25][26] In temperate habitats, for instance, honey bee colonies routinely perform the waggle dance, but can still successfully forage when the dance is experimentally obscured. In tropical habitats, honey bee foraging is severely impaired if waggle dancing is prevented. This is thought to be due to the patchiness of resources in tropical environment versus the homogeneity of resources in temperate environments. In the tropics, food resources can come in the form of flowering trees which are rich in nectar but are scattered sparsely and bloom only briefly. Thus, in tropical zones information about forage location might be more valuable than in temperate zones.[19]
Evolution[edit]
Ancestors to modern honeybees most likely performed excitatory movements to encourage other nestmates to forage. These excitatory movements include shaking, zig-zagging, buzzing and crashing into nestmates. Similar behavior is observed in other Hymenoptera including stingless bees, wasps, bumblebees and ants.[17]
The waggle dance is thought to have evolved to aid in communicating information about a new nest site, rather than spatial information about foraging sites.[17]
Observations have suggested that different species of honeybees have different "dialects" of the waggle dance, each species or subspecies dance varying by curve or duration.[27][28] A study from 2008 demonstrated that a mixed colony of Asiatic honeybees (Apis cerana cerana) and European honeybees (Apis mellifera ligustica) were gradually able to understand one another's "dialects" of waggle dance.[29]
Applications to operations research[edit]
In line with recent work in swarm intelligence research involving optimization algorithms inspired by the behavior of social insects (including bees, ants and termites), and vertebrates such as fish and birds, there has recently been research on using bee waggle dance behavior for efficient fault-tolerant routing.[30] From the abstract of Wedde, Farooq, and Zhang (2004):[31]
In this paper we present a novel routing algorithm, BeeHive, which has been inspired by the communicative and evaluative methods and procedures of honey bees. In this algorithm, bee agents travel through network regions called foraging zones. On their way their information on the network state is delivered for updating the local routing tables. BeeHive is fault tolerant, scalable, and relies completely on local, or regional, information, respectively. We demonstrate through extensive simulations that BeeHive achieves a similar or better performance compared to state-of-the-art algorithms.
Another bee-inspired stigmergic computational technique called bee colony optimization is employed in Internet Server Optimization.[32][33]
The Zigbee RF protocol is named after the waggle dance.
See also[edit]
Animal communication
Bee learning and communication
Tremble dance
Grooming dance
Wasps
References[edit]
^ Jump up to: a b Riley, J.; Greggers, U.; Smith, A.; Reynolds, D.; Menzel, R. (2005). "The flight paths of honeybees recruited by the waggle dance". Nature. 435 (7039): 205–207. Bibcode:2005Natur.435..205R. doi:10.1038/nature03526. PMID 15889092.
Jump up ^ Seeley T.D.; Visscher P.K.; Passino K.M. (2006). "Group decision making in honey bee swarms". American Scientist. 94: 220–229. doi:10.1511/2006.3.220.
Jump up ^ Grüter, Christoph; Farina, Walter M. (May 2009). "The honeybee waggle dance: can we follow the steps?". Trends in Ecology & Evolution. 24 (5): 242–247. doi:10.1016/j.tree.2008.12.007. PMID 19307042.
Jump up ^ Gardner, Kathryn E.; Seeley, Thomas D.; Calderone, Nicholas W. (2008-04-01). "Do honeybees have two discrete dances to advertise food sources?". Animal Behaviour. 75 (4): 1291–1300. doi:10.1016/j.anbehav.2007.09.032.
^ Jump up to: a b c Frisch, Karl von. (1967) The Dance Language and Orientation of Bees. Cambridge, Mass.: The Belknap Press of Harvard University Press.
Jump up ^ Thom, C.; Gilley, D.; Hooper, J.; Esch, H. (2007). "The scent of the waggle dance". PLoS Biology. 5 (9): e228. doi:10.1371/journal.pbio.0050228. PMC 1994260  . PMID 17713987.
Jump up ^ "The Waggle Dance". www.pbs.org. Retrieved 2016-01-27.
Jump up ^ Radloff, Sara E.; Hepburn, H. Randall; Engel, Michael S. (2011). Honeybees of Asia. Berlin: Springer Science & Business Media. ISBN 978-3642164217.
Jump up ^ Raffiudin, Rika; Crozier, Ross H. (2007-05-01). "Phylogenetic analysis of honey bee behavioral evolution". Molecular Phylogenetics and Evolution. 43 (2): 543–552. doi:10.1016/j.ympev.2006.10.013.
Jump up ^ Bozic, J.; Abramson, C.; Bedencic, M. (2006). "Reduced ability of ethanol drinkers for social communication in honeybees (Apis mellifera carnica Poll.)". Alcohol (Fayetteville, N.Y.). 38 (3): 179–183. doi:10.1016/j.alcohol.2006.01.005. PMID 16905444.
Jump up ^ Walker, Matt (31 July 2009). "Honeybees warn of Risky Flowers". BBC Earth News. Retrieved 18 January 2010.
Jump up ^ Abbott, K. R.; Dukas, R. (2009). "Honeybees consider flower danger in their waggle dance". Animal Behaviour. 78 (3): 633–635. doi:10.1016/j.anbehav.2009.05.029.
Jump up ^ Aristotle, Historia animalium, IX, 40, Becker 624b; modified from the translation by D.W. Thompson in The Works of Aristotle, Clarendon, Oxford, 1910.
Jump up ^ Greggers, Uwe; Koch G; Schmidt V; Dürr A; Floriou-Servou A; Piepenbrock D; Göpfert MC; Menzel R (March 2013). "Reception and learning of electric fields". Proceedings of the Royal Society B. 280: 20130528. doi:10.1098/rspb.2013.0528. PMC 3619523  . PMID 23536603.
^ Jump up to: a b c Grüter, C.; Balbuena, M.; Farina, W. (2008). "Informational conflicts created by the waggle dance". Proceedings: Biological Sciences. 275 (1640): 1321–1327. doi:10.1098/rspb.2008.0186. PMC 2602683  . PMID 18331980.
Jump up ^ Kirchner, Wolfgang. "Acoustic signals in the dance language of the giant honeybee, Apis dorsata". Behavior Ecology and Sociobiology (33): 67–72.
^ Jump up to: a b c d e Grüter, C.; Farina, W. (2009). "The honeybee waggle dance: can we follow the steps?". Trends in Ecology & Evolution. 24 (5): 242–247. doi:10.1016/j.tree.2008.12.007. PMID 19307042.
Jump up ^ Saussure, Ferdinand de (1916), "Nature of the Linguistics Sign", in: Charles Bally & Albert Sechehaye (Ed.), Cours de linguistique générale, McGraw Hill Education.
^ Jump up to: a b Dornhaus, A.; Chittka, L. (2004). "Why do honey bees dance?". Behavioral Ecology and Sociobiology. 55 (4): 395–401. doi:10.1007/s00265-003-0726-9.
Jump up ^ Gruter, C.; Balbuena, M. S.; Farina, W. M. (2008). ". Informational conflicts created by the waggle dance". Proceedings of the Royal Society B: Biological Sciences. 275: 1321–1327. doi:10.1098/rspb.2008.0186. PMC 2602683  . PMID 18331980.
Jump up ^ Al Toufailia, H.; Gruter, C.; Ratnieks, F. L. W. (2013). "Persistence to unrewarding feeding locations by honeybee foragers (Apis mellifera): the effects of experience, resource profitability and season". Ethology. 119: 1096–1106. doi:10.1111/eth.12170.
Jump up ^ Gruter, C; Ratnieks, F. L. W. (2011). "Honeybee foragers increase the use of waggle dance information when private information becomes unrewarding". Animal Behaviour. 81: 949–954. doi:10.1016/j.anbehav.2011.01.014.
Jump up ^ Gruter, C.; Farina, W. M. (2009). "The honeybee waggle dance: can we follow the steps?". Trends in Ecology & Evolution. 24: 242–247. doi:10.1016/j.tree.2008.12.007. PMID 19307042.
Jump up ^ name=Persistence to unrewarding feeding locations by honeybee foragers (Apis mellifera): the effects of experience, resource profitability and season"
Jump up ^ name="The biology of the dance language"
Jump up ^ name="Informational conflicts created by the waggle dance"
Jump up ^ Gould; Towne (1989). "On the Evolution of the Dance Language: Response to Dyer and Seeley". American Naturalist. The American Society of Naturalists. 134 (1): 156–159. doi:10.1086/284972. JSTOR 2462282.
Jump up ^ Dyer; Seeley (1991). "Dance Dialects and Foraging Range in Three Asian Honey Bee Species". Behavioral Ecology and Sociobiology. Springer. 28 (4): 227–233. doi:10.1007/BF00175094. JSTOR 4600541.
Jump up ^ Su, S.; Cai, F.; Si, A.; Zhang, S.; Tautz, J.; Chen, S.; Giurfa, M. (2008). Giurfa, Martin, ed. "East learns from West: Asiatic honeybees can understand dance language of European honeybees". PLoS ONE. 3 (6): e2365. Bibcode:2008PLoSO...3.2365S. doi:10.1371/journal.pone.0002365. PMC 2391287  . PMID 18523550.
Jump up ^ Crina, Grosan; Abraham Ajith. (2006) Stigmergic Optimization: Inspiration, Technologies and Perspectives. Studies in Computational Intelligence. Vol. 31. pp. 1-24. Springer Berlin / Heidelberg. ISBN 978-3-540-34689-0
Jump up ^ Wedde, H. F.; Farooq, M.; Pannenbaecker, T.; Vogel, B.; Mueller, C.; Meth, J.; Jeruschkat, R. (2005). "BeeAdHoc". Proceedings of the 2005 conference on Genetic and evolutionary computation - GECCO '05. p. 153. doi:10.1145/1068009.1068034. ISBN 1595930108.
Jump up ^ Nakrani, S.; Tovey, C. (2004). "On Honey Bees and Dynamic Server Allocation in Internet Hosting Centers". Adaptive Behavior. 12 (3–4): 223–240. doi:10.1177/105971230401200308.
Jump up ^ C. Tovey, (2004) "The Honey Bee Algorithm: A Biological Inspired Approach to Internet Server Optimization". Engineering Enterprise. Spring 2004, pp.13-15.
Further reading[edit]
Gould JL (1975). "Honey bee recruitment: the dance-language controversy" (PDF). Science. 189 (4204): 685–693. doi:10.1126/science.1154023.
Riley JR, Greggers U, Smith AD, Reynolds DR, Menzel R (2005). "The flight paths of honeybees recruited by the waggle dance". Nature. 435 (7039): 205–207. Bibcode:2005Natur.435..205R. doi:10.1038/nature03526. PMID 15889092.
Seeley TD (1995). The Wisdom of the Hive. Cambridge, MA: Harvard University Press.
von Frisch K (1967). The Dance Language and Orientation of Bees. Cambridge, MA: Harvard University Press.
Rendell, L; Boyd, R.; Cownden, D; Enquist, M.; Eriksson, K.; Feldman, W. M.; Fogarty, L.; Ghirlanda, S.; Lilicrap, T.; Laland, K. N. (2010). "Why copy others? Insights from the social learning strategies tournament". Science. 328: 208–213. doi:10.1126/science.1184719. PMC 2989663  . PMID 20378813.
Gruter, C; Ratnieks, F. L. (2011). "Honeybee foragers increase the use of waggle dance information when private information becomes unrewarding". Animal Behaviour. 81: 949–954. doi:10.1016/j.anbehav.2011.01.014.
Dyer, F. C. (2002). "The biology of the dance language". Annual Review of Entomology. 47: 917–949. doi:10.1146/annurev.ento.47.091201.145306.
Beekman, M.; Golag, R. S.; Even, N.; Wattanchiyingchareon, W.; Olroyd, B. P. (2008). "Dance precision of Apis florae--clues to the evolution of honeybee dance language". Behavioral Ecology and Sociobiology. 62: 1259–1265. doi:10.1007/s00265-008-0554-z.
Al Toufalia, H. M. (2012). "Honey bee foraging: persistence to non-rewarding feeding locations and waggle dance communication". Doctoral thesis, University of Sussexx.
External links[edit]
Wikimedia Commons has media related to Waggle dance.
NATURE, Silence of the Bees, Inside the Hive, PBS on YouTube
Waggle Dance Infographic - VetSci
Communication and Recruitment to Food Sources by Apis mellifera — USDA-ARS (accessed 2005-03)
Honeybee Communication — Kimball's Biology Pages (accessed 2005-09)
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Disulfide
From Wikipedia, the free encyclopedia
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In chemistry, a disulfide refers to a functional group with the structure R−S−S−R′. The linkage is also called an SS-bond or sometimes a disulfide bridge and is usually derived by the coupling of two thiol groups. The connection is a persulfide, in analogy to its congener, peroxide (R−O−O−R′), but this terminology is rarely used, except in reference to hydrodisulfides (R−S−S−H compounds).
In inorganic chemistry disulfide usually refers to the corresponding anion S2−
2 (−S−S−), for example in disulfur dichloride.
Contents
[hide]
1 Organic disulfides
1.1 Properties
1.2 Synthesis
1.3 Reactions
1.4 Occurrence in proteins
1.4.1 Predicting disulfide abundance
1.4.2 In bacteria and archaea
1.4.3 In eukaryotes
1.4.4 Disulfides in regulatory proteins
1.4.5 In hair and feathers
2 Inorganic disulfides
3 In industry
4 Related compounds
4.1 Misnomers
5 References
6 Further reading
Organic disulfides[edit]
A selection of disulfides
FeS2,
"fool's gold" S2Cl2,
a common industrial chemical cystine,
crosslinker in many proteins lipoic acid,
a vitamin Ph2S2,
a common organic disulfide
Properties[edit]
The disulfide bonds are strong, with a typical bond dissociation energy of 60 kcal/mol (251 kJ mol−1). However, being about 40% weaker than C−C and C−H bonds, the disulfide bond is often the "weak link" in many molecules. Furthermore, reflecting the polarizability of divalent sulfur, the S−S bond is susceptible to scission by polar reagents, both electrophiles and especially nucleophiles (Nu):[1]
RS−SR + Nu− → RS−Nu + RS−
The disulfide bond is about 2.05 Å in length, about 0.5 Å longer than a C−C bond. Rotation about the S−S axis is subject to a low barrier. Disulfides show a distinct preference for dihedral angles approaching 90°. When the angle approaches 0° or 180°, then the disulfide is a significantly better oxidant.
Disulfides where the two R groups are the same are called symmetric, examples being diphenyl disulfide and dimethyl disulfide. When the two R groups are not identical, the compound is said to be an asymmetric or mixed disulfide.[2]
Although the hydrogenation of disulfides is usually not practical, the equilibrium constant for the reaction provides a measure of the standard redox potential for disulfides:
RSSR + H2 → 2 RSH
This value is about −250 mV versus the standard hydrogen electrode (pH = 7). By comparison, the standard reduction potential for ferrodoxins is about −430 mV.
Synthesis[edit]
Disulfide bonds are usually formed from the oxidation of sulfhydryl (−SH) groups, especially in biological contexts.[3] The transformation is depicted as follows:
2 RSH ⇌ RS−SR + 2 H+ + 2 e−
A variety of oxidants participate in this reaction including oxygen and hydrogen peroxide. Such reactions are thought to proceed via sulfenic acid intermediates. In the laboratory, iodine in the presence of base is commonly employed to oxidize thiols to disulfides. Several metals, such as copper(II) and iron(III) complexes affect this reaction.[citation needed] Alternatively, disulfide bonds in proteins often formed by thiol-disulfide exchange:
RS−SR + R′SH ⇌ R′S−SR + RSH
Such reactions are mediated by enzymes in some cases and in other cases are under equilibrium control, especially in the presence of a catalytic amount of base.
The alkylation of alkali metal di- and polysulfides gives disulfides. "Thiokol" polymers arise when sodium polysulfide is treated with an alkyl dihalide. In the converse reaction, carbanionic reagents react with elemental sulfur to afford mixtures of the thioether, disulfide, and higher polysulfides. These reactions are often unselective but can be optimized for specific applications.
Many specialized methods have been developed for forming disulfides, usually for applications in organic synthesis. Reagents that deliver the equivalent of "RS+" react with thiols to give asymmetrical disulfides:[3]
RSH + R′SNR″2 → RS−SR′ + HNR″2
where R″2N is the phthalimido group.
Reactions[edit]
The most important aspect of disulfide bonds is their cleavage, which occurs via reduction. A variety of reductants can be used. In biochemistry, thiols such as β-mercaptoethanol (β-ME) or dithiothreitol (DTT) serve as reductants; the thiol reagents are used in excess to drive the equilibrium to the right:
RS−SR + 2 HOCH2CH2SH ⇌ HOCH2CH2S−SCH2CH2OH + 2 RSH
The reductant tris(2-carboxyethyl)phosphine (TCEP) is useful, beside being odorless compared to β-ME and DTT, because it is selective, working at both alkaline and acidic conditions (unlike DTT), is more hydrophilic and more resistant to oxidation in air. Furthermore, it is often not needed to remove TCEP before modification of protein thiols.[4]
In organic synthesis, hydride agents are typically employed for scission of disulfides, such as sodium borohydride. More aggressive, alkali metals will effect this reaction:
RS−SR + 2 Na → 2 NaSR
These reactions are often followed by protonation of the resulting metal thiolate:
NaSR + HCl → HSR + NaCl
Thiol–disulfide exchange is a chemical reaction in which a thiolate group −S− attacks a sulfur atom of a disulfide bond −S−S−. The original disulfide bond is broken, and its other sulfur atom (green atom in Figure 1) is released as a new thiolate, carrying away the negative charge. Meanwhile, a new disulfide bond forms between the attacking thiolate (red atom in Figure 1) and the original sulfur atom (blue atom in Figure 1).[5][6]
Figure 1. Thiol–disulfide exchange showing the linear intermediate in which the charge is shared among the three sulfur atoms. The thiolate group (shown in red) attacks a sulfur atom (shown in blue) of the disulfide bond, displacing the other sulfur atom (shown in green) and forming a new disulfide bond.
Thiolates, not thiols, attack disulfide bonds. Hence, thiol–disulfide exchange is inhibited at low pH (typically, below 8) where the protonated thiol form is favored relative to the deprotonated thiolate form. (The pKa of a typical thiol group is roughly 8.3, but can vary due to its environment.)
Thiol–disulfide exchange is the principal reaction by which disulfide bonds are formed and rearranged in a protein. The rearrangement of disulfide bonds within a protein generally occurs via intra-protein thiol–disulfide exchange reactions; a thiolate group of a cysteine residue attacks one of the protein's own disulfide bonds. This process of disulfide rearrangement (known as disulfide shuffling) does not change the number of disulfide bonds within a protein, merely their location (i.e., which cysteines are bonded). Disulfide reshuffling is generally much faster than oxidation/reduction reactions, which change the number of disulfide bonds within a protein. The oxidation and reduction of protein disulfide bonds in vitro also generally occurs via thiol–disulfide exchange reactions. Typically, the thiolate of a redox reagent such as glutathione or dithiothreitol attacks the disulfide bond on a protein forming a mixed disulfide bond between the protein and the reagent. This mixed disulfide bond when attacked by another thiolate from the reagent, leaves the cysteine oxidized. In effect, the disulfide bond is transferred from the protein to the reagent in two steps, both thiol–disulfide exchange reactions.
The in vivo oxidation and reduction of protein disulfide bonds by thiol–disulfide exchange is facilitated by a protein called thioredoxin. This small protein, essential in all known organisms, contains two cysteine amino acid residues in a vicinal arrangement (i.e., next to each other), which allows it to form an internal disulfide bond, or disulfide bonds with other proteins. As such, it can be used as a repository of reduced or oxidized disulfide bond moieties.
Many specialized organic reactions have been developed for disulfides, again mainly associated with the scission of the S−S bond, which is usually the weakest bond in a molecule. In the Zincke disulfide cleavage reactions, disulfides are cleaved to give a sulfenyl halide by reaction with bromine or chlorine.[clarification needed][7][8]
Figure 2. Disulfide bonds (schematic presentation) in a protein.
Occurrence in proteins[edit]
Disulfide bonds play an important role in the folding and stability of some proteins, usually proteins secreted to the extracellular medium.[2] Since most cellular compartments are reducing environments, in general, disulfide bonds are unstable in the cytosol, with some exceptions as noted below, unless a sulfhydryl oxidase is present.[9]
Figure 3. Cystine is composed of two cysteines linked by a disulfide bond (shown here in its neutral form).
Disulfide bonds in proteins are formed between the thiol groups of cysteine residues by the process of oxidative folding. The other sulfur-containing amino acid, methionine, cannot form disulfide bonds. A disulfide bond is typically denoted by hyphenating the abbreviations for cysteine, e.g., when referring to ribonuclease A the "Cys26–Cys84 disulfide bond", or the "26–84 disulfide bond", or most simply as "C26–C84"[10] where the disulfide bond is understood and does not need to be mentioned. The prototype of a protein disulfide bond is the two-amino-acid peptide cystine, which is composed of two cysteine amino acids joined by a disulfide bond (shown in Figure 3 in its unionized form). The structure of a disulfide bond can be described by its χss dihedral angle between the Cβ−Sγ−Sγ−Cβ atoms, which is usually close to ±90°.
The disulfide bond stabilizes the folded form of a protein in several ways:
It holds two portions of the protein together, biasing the protein towards the folded topology. That is, the disulfide bond destabilizes the unfolded form of the protein by lowering its entropy.
The disulfide bond may form the nucleus of a hydrophobic core of the folded protein, i.e., local hydrophobic residues may condense around the disulfide bond and onto each other through hydrophobic interactions.
Related to 1 and 2, the disulfide bond link two segments of the protein chain, the disulfide bond increases the effective local concentration of protein residues and lowers the effective local concentration of water molecules. Since water molecules attack amide-amide hydrogen bonds and break up secondary structure, a disulfide bond stabilizes secondary structure in its vicinity. For example, researchers have identified several pairs of peptides that are unstructured in isolation, but adopt stable secondary and tertiary structure upon forming a disulfide bond between them.
A disulfide species is a particular pairing of cysteines in a disulfide-bonded protein and is usually depicted by listing the disulfide bonds in parentheses, e.g., the "(26–84, 58–110) disulfide species". A disulfide ensemble is a grouping of all disulfide species with the same number of disulfide bonds, and is usually denoted as the 1S ensemble, the 2S ensemble, etc. for disulfide species having one, two, etc. disulfide bonds. Thus, the (26–84) disulfide species belongs to the 1S ensemble, whereas the (26–84, 58–110) species belongs to the 2S ensemble. The single species with no disulfide bonds is usually denoted as R for "fully reduced". Under typical conditions, disulfide reshuffling is much faster than the formation of new disulfide bonds or their reduction; hence, the disulfide species within an ensemble equilibrate more quickly than between ensembles.
The native form of a protein is usually a single disulfide species, although some proteins may cycle between a few disulfide states as part of their function, e.g., thioredoxin. In proteins with more than two cysteines, non-native disulfide species may be formed, which are almost always misfolded. As the number of cysteines increases, the number of nonnative species increases factorially.
Predicting disulfide abundance[edit]
The number of ways i in which p disulfide bonds can be formed from n cysteine residues present in a protein is given by the formula
i = n ! ( n − 2 p ) ! p ! 2 p {\displaystyle i={\frac {n!}{(n-2p)!\,p!\,2^{p}}}}
Here,
i is the number of different disulfide bond isomers or connectivities possible.
n is the number of cysteines present in the protein molecule.
p is the number of disulphide bonds that are formed (hence 2p is less than or equal to n).
The above formula is the most general relation which can be used to calculate the number of possible disulfide bond isomers (or connectivities) when n is either even or odd, and when all or only some of the cysteines are involved in the formation of disulfide bonds.
However, many of the naturally occurring proteins that have disulfide bonds possess an even number of cysteines with all of the cysteines participating in the formation of disulfide bonds. For this specific case, n is an even number and p is equal to n/2. Substituting the value of p, the above formula for the possible number of disulfide bond connectivities simplifies to:
i = n ! ( n − 2 p ) ! p ! 2 p = n ! ( n − 2 ( n 2 ) ) ! ( n 2 ) ! 2 n 2 = n ! ( n 2 ) ! 2 n 2 {\displaystyle {\begin{aligned}i&={\frac {n!}{(n-2p)!\,p!\,2^{p}}}\\&={\frac {n!}{\left(n-2\left({\frac {n}{2}}\right)\right)!\,{\left({\frac {n}{2}}\right)}!\,{2^{\frac {n}{2}}}}}\\&={\frac {n!}{{\left({\frac {n}{2}}\right)}!\,{2^{\frac {n}{2}}}}}\end{aligned}}}
For this particular case (n is even and all cysteines form disulfide bonds), a formula which is more easier to remember is given by:
i = ( n − 1 ) ( n − 3 ) ( n − 5 ) ⋯ 1 {\displaystyle i=(n-1)\,(n-3)\,(n-5)\,\cdots 1}
Both of the above relations hold good for the proteins which have an even number of cysteines and all the cysteines are involved in the formation of disulfide bonds. Both of the above formulae are derived using the same logic and essentially represent a simplification of the same starting formula.
As a specific example for the above case, an eight-cysteine protein such as ribonuclease A can form 105 different four-disulfide species when all the cysteines are involved in the formation of disulfide bonds. Here n = 8 and p = 4.
So, here
i = ( 8 − 1 ) ( 8 − 3 ) ( 8 − 5 ) ( 8 − 7 ) = 7 ⋅ 5 ⋅ 3 ⋅ 1 = 105 {\displaystyle i=(8-1)\,(8-3)\,(8-5)\,(8-7)=7\cdot 5\cdot 3\cdot 1=105}
Only one of the 105 possible isomers is the native disulfide species. Isomerases have been identified that catalyze the interconversion of disulfide species, accelerating the formation of the native disulfide species.
Disulfide species that have only native disulfide bonds (but not all of them) are denoted by "des" followed by the lacking native disulfide bond(s) in square brackets. For example, the des[40–95] disulfide species has all the native disulfide bonds except that between cysteines 40 and 95. Disulfide species that lack one native disulfide bond are frequently folded, in particular, if the missing disulfide bond is exposed to solvent in the folded, native protein.
In order to analyze the structure of proteins, it is often necessary to break disulfide bonds. This reduction of disulfide bonds can be accomplished by treatment with 2-mercaptoethanol, dithiothreitol, or tris(2-carboxyethyl)phosphine.
In bacteria and archaea[edit]
Disulfide bonds play an important protective role for bacteria as a reversible switch that turns a protein on or off when bacterial cells are exposed to oxidation reactions. Hydrogen peroxide (H2O2) in particular could severely damage DNA and kill the bacterium at low concentrations if not for the protective action of the SS-bond. Archaea typically have fewer disulfides than higher organisms.[11]
In eukaryotes[edit]
In eukaryotic cells, in general, stable disulfide bonds are formed in the lumen of the RER (rough endoplasmic reticulum) and the mitochondrial intermembrane space but not in the cytosol. This is due to the more oxidizing environment of the aforementioned compartments and more reducing environment of the cytosol (see glutathione). Thus disulfide bonds are mostly found in secretory proteins, lysosomal proteins, and the exoplasmic domains of membrane proteins.
There are notable exceptions to this rule. For example, many nuclear and cytosolic proteins can become disulfide-crosslinked during necrotic cell death.[12] Similarly, a number of cytosolic proteins which have cysteine residues in proximity to each other that function as oxidation sensors or redox catalysts; when the reductive potential of the cell fails, they oxidize and trigger cellular response mechanisms. The virus Vaccinia also produces cytosolic proteins and peptides that have many disulfide bonds; although the reason for this is unknown presumably they have protective effects against intracellular proteolysis machinery.
Disulfide bonds are also formed within and between protamines in the sperm chromatin of many mammalian species.
Disulfides in regulatory proteins[edit]
As disulfide bonds can be reversibly reduced and re-oxidized, the redox state of these bonds has evolved into a signaling element. In chloroplasts, for example, the enzymatic reduction of disulfide bonds has been linked to the control of numerous metabolic pathways as well as gene expression. The reductive signaling activity has been shown, thus far, to be carried by the ferredoxin thioredoxin system, channeling electrons from the light reactions of photosystem I to catalytically reduce disulfides in regulated proteins in a light dependent manner. In this way chloroplasts adjust the activity of key processes such as the Calvin–Benson cycle, starch degradation, ATP production and gene expression according to light intensity.
In hair and feathers[edit]
Over 90% of the dry weight of hair comprises proteins called keratins, which have a high disulfide content, from the amino acid cysteine. The robustness conferred in part by disulfide linkages is illustrated by the recovery of virtually intact hair from ancient Egyptian tombs. Feathers have similar keratins and are extremely resistant to protein digestive enzymes. Different parts of the hair and feather have different cysteine levels, leading to harder or softer material. Manipulating disulfide bonds in hair is the basis for the permanent wave in hairstyling. Reagents that affect the making and breaking of S−S bonds are key, e.g., ammonium thioglycolate. The high disulfide content of feathers dictates the high sulfur content of bird eggs. The high sulfur content of hair and feathers contributes to the disagreeable odor that results when they are burned.
Inorganic disulfides[edit]
The disulfide anion is S2−
2, or −S−S−. Sulfur is usually assigned to the reduced oxidation number −2, described as S2− and called sulfide. It has the electron configuration of a noble gas (argon). In disulfide, sulfur is only reduced to a state with oxidation number −1. Its configuration then resembles that of a chlorine atom. It thus tends to form a covalent bond with another S− center to form S2−
2 group. Oxygen also behaves similarly, e.g. in peroxides such as H2O2. Examples:
Iron disulfide (FeS2), e.g. the mineral pyrite (V(S2)2 — patronite).
Disulfur dichloride (S2Cl2), a distillable liquid.
In industry[edit]
Disulfide and (polysulfide) bonds are the crosslinking groups that result from the vulcanization of rubber. In analogy to the role of disulfides in proteins, the S−S linkages in rubber are crosslinkers, and strongly affect the rheology of the material.
Related compounds[edit]
Thiosulfoxides are orthogonally isomeric with disulfides, having the second sulfur branching from the first and not partaking in a continuous chain, i.e. >S=S rather than −S−S−.
Disulfide bonds are analogous but more common than related peroxides and diselenide bonds. Intermediate compounds of these also exist, for example, thioperoxides, also known as oxaulfide bonds, have formula R1OSR2 (equivalently R2SOR1). These are isomeric to sulfoxides in a similar manner to the above; i.e. >S=O rather than −S−O−.
Thiuram disulfides, with the formula (R2NCSS)2, are disulfides but they behave distinctly because of the thiocarbonyl group.
Compounds with three sulfur atoms, such as CH3S−S−SCH3, are called trisulfides, or trisulfide bonds.
Misnomers[edit]
Disulfide is also used to refer to compounds that contain two sulfide (S2−) centers. The compound carbon disulfide, CS2 is described with the structural formula i.e. S=C=S. This molecule is not a disulfide in the sense that it lacks a S-S bond. Similarly, molybdenum disulfide, MoS2, is not a disulfide in the sense again that its sulfur atoms are not linked.
CS2 MoS2
References[edit]
This article needs additional citations for verification. Please help improve this article by adding citations to reliable sources. Unsourced material may be challenged and removed. (September 2015) (Learn how and when to remove this template message)
Jump up ^ Cremlyn, R. J. (1996). An Introduction to Organosulfur Chemistry. Chichester: John Wiley and Sons. ISBN 0-471-95512-4.
^ Jump up to: a b Sevier, C. S.; Kaiser, C. A. (2002). "Formation and transfer of disulphide bonds in living cells". Nature Reviews Molecular Cell Biology . 3 (11): 836–847. doi:10.1038/nrm954. PMID 12415301.
^ Jump up to: a b Witt, D. (2008). "Recent developments in disulfide bond formation". Synthesis. 2008 (16): 2491–2509. doi:10.1055/s-2008-1067188.
Jump up ^ TCEP technical information, from Interchim
Jump up ^ Gilbert, H. F. (1990). "Molecular and Cellular Aspects of Thiol–Disulfide Exchange". Advances in Enzymology. 63: 69–172. doi:10.1002/9780470123096.ch2. PMID 2407068.
Jump up ^ Gilbert, H. F. (1995). "Thiol/disulfide exchange equilibria and disulfide bond stability". Methods in Enzymology. 251: 8–28. doi:10.1016/0076-6879(95)51107-5. PMID 7651233.
Jump up ^ For example the conversion of di-o-nitrophenyl disulfide to o-nitrophenylsulfur chloride Hubacher, Max H. (1943). "o-Nitrophenylsulfur chloride". Organic Syntheses. ; Collective Volume, 2, p. 455
Jump up ^ Methyl sulfenyl chloride: Douglass, Irwin B.; Norton, Richard V. (1973). "Methanesulfinyl Chloride". Organic Syntheses. ; Collective Volume, 5, p. 709
Jump up ^ Hatahet, F.; Nguyen, V. D.; Salo, K. E.; Ruddock, L. W. (2010). "Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. coli". Microbial Cell Factories. 9 (67): 67. doi:10.1186/1475-2859-9-67. PMC 2946281  . PMID 20836848.
Jump up ^ Ruoppolo, M.; Vinci, F.; Klink, T. A.; Raines, R. T.; Marino, G. (2000). "Contribution of individual disulfide bonds to the oxidative folding of ribonuclease A". Biochemistry. 39 (39): 12033–12042. doi:10.1021/bi001044n. PMID 11009618.
Jump up ^ Ladenstein, R.; Ren, B. (2008). "Reconsideration of an early dogma, saying "there is no evidence for disulfide bonds in proteins from archaea"". Extremophiles. 12 (1): 29–38. doi:10.1007/s00792-007-0076-z. PMID 17508126.
Jump up ^ Samson, Andre L.; Knaupp, Anja S.; Sashindranath, Maithili; Borg, Rachael J.; Au, Amanda E.-L.; Cops, Elisa J.; Saunders, Helen M.; Cody, Stephen H.; McLean, Catriona A. (2012-10-25). "Nucleocytoplasmic coagulation: an injury-induced aggregation event that disulfide crosslinks proteins and facilitates their removal by plasmin". Cell Reports. 2 (4): 889–901. doi:10.1016/j.celrep.2012.08.026. ISSN 2211-1247. PMID 23041318.
Further reading[edit]
Sela, M.; Lifson, S. (1959). "The reformation of disulfide bridges in proteins". Biochimica et Biophysica Acta. 36 (2): 471–478. doi:10.1016/0006-3002(59)90188-X. PMID 14444674.
Stark, G. R.; Stern, K.; Atala, A.; Yoo, J. (1977). "Cleavage at cysteine after cyanylation". Methods in Enzymology. 47 (2): 129–132. doi:10.1016/j.ymeth.2008.09.005. PMID 927170.
Thornton, J. M. (1981). "Disulphide bridges in globular proteins". Journal of Molecular Biology. 151 (2): 261–287. doi:10.1016/0022-2836(81)90515-5. PMID 7338898.
Thannhauser, T. W.; Konishi, Y.; Scheraga, H. A. (1984). "Sensitive quantitative analysis of disulfide bonds in polypeptides and proteins". Analytical Biochemistry. 138 (1): 181–188. doi:10.1016/0003-2697(84)90786-3. PMID 6547275.
Wu, J.; Watson, J. T. (1998). "Optimization of the cleavage reaction for cyanylated cysteinyl proteins for efficient and simplified mass mapping". Analytical Biochemistry. 258 (2): 268–276. doi:10.1006/abio.1998.2596. PMID 9570840.
Futami, J.; Tada, H.; Seno, M.; Ishikami, S.; Yamada, H. (2000). "Stabilization of human RNAse 1 by introduction of a disulfide bond between residues 4 and 118". Journal of Biochemistry. 128 (2): 245–250. doi:10.1093/oxfordjournals.jbchem.a022747. PMID 10920260.
Wittenberg, G.; Danon, A. (2008). "Disulfide bond formation in chloroplasts: Formation of disulfide bonds in signaling chloroplast proteins". Plant Science. 175 (4): 459–466. doi:10.1016/j.plantsci.2008.05.011.
Kadokura, Hiroshi; Katzen, Federico; Beckwith, Jon (2003). "Protein Disulfide Bond Formation in Prokaryotes". Annual Review of Biochemistry. 72 (1): 111–135. doi:10.1146/annurev.biochem.72.121801.161459. PMID 12524212.
Tu, B. P.; Weissman, J. S. (2004). "Oxidative protein folding in eukaryotes: mechanisms and consequences". The Journal of Cell Biology. 164 (3): 341–346. doi:10.1083/jcb.200311055. PMC 2172237  . PMID 14757749.
Ellgaard, Lars; Ruddock, Lloyd W. (2005). "The human protein disulphide isomerase family: substrate interactions and functional properties". EMBO Reports. 6 (1): 28–32. doi:10.1038/sj.embor.7400311. PMC 1299221  . PMID 15643448.
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List of banks in India
From Wikipedia, the free encyclopedia
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The following is a list of banks in India:
Contents
1 Cooperative banks.
1.1 State Cooperative Banks (SCBs)
1.2 Urban Cooperative Banks (UCBs)
2 Foreign Banks
2.1 Foreign Banks with branches in India
2.2 Foreign Banks with representative offices in India
3 Local Area Banks
4 Payments Banks
5 Private-Sector Banks
6 Public-Sector Bank
7 Regional Rural Banks (RRBs)
8 Small Finance Banks
9 See also
10 References
11 External links
Cooperative banks.[edit]
State Cooperative Banks (SCBs)[edit]
List of State Cooperative Banks in India:
Andaman and Nicobar State Co-operative Bank
AP State Co-operative Bank
Arunachal Pradesh State Co-operative Apex Bank
Assam Co-operative Apex Bank
Bihar State Co-operative Bank
Chandigarh State Co-operative Bank
Chhattisgarh Rajya Sahakari Bank Maryadit
Delhi State Co-operative Bank
Goa State Co-operative Bank ltd
Gujarat State Cooperative Agriculture and Rural Development Bank Ltd.
Gujarat State Co-operative Bank
Haryana State Co-operative Apex Bank
Himachal Pradesh State Co-operative Bank
Jammu and Kashmir State Co-operative Bank
Jharkhand State Co-operative Bank
Karnataka State Co-operative Apex Bank Bangalore
Kerala State Co-operative Bank
Madhya Pradesh Rajya Sahakari Bank Maryadit
Maharashtra State Co-operative Bank
Manipur State Co-operative Bank
Meghalaya Co-operative Apex Bank
Mizoram Co-operative Apex Bank
Nagaland State Co-operative Bank
Odisha State Co-Operative Bank
Pondichery State Co-operative Bank
Punjab State Co-operative Bank
Rajasthan State Co-operative Bank
Sikkim State Co-operative Bank
The Tamil Nadu State Apex Co-operative Bank
Telangana State Co-Operative Apex Bank Limited
Tripura State Co-operative Bank
Uttar Pradesh Co-operative Bank
Uttarakhand State Co-operative Bank
West Bengal State Co-operative Bank
Urban Cooperative Banks (UCBs)[edit]
List of Scheduled Urban Cooperative Banks in India:
Abhyudaya Co-operative Bank
Adhyapaka Urban Co-operative Bank
Akhand Anand Co-Op Bank
Akola Janata Commercial Co-operative Bank
Akola Urban Co-operative Bank
Ahmedabad Mercantile Co-Op Bank
Andhra Pradesh Mahesh Co-Op Urban Bank
Apna Sahakari Co-Op Bank Ltd
Bassein Catholic Co-operative Bank
Bharat Co-operative Bank (Mumbai)
Bharati Sahakari Bank
Bombay Mercantile Co-operative Bank
Citizencredit Co-operative Bank
Dombivli Nagari Sahakari Bank Ltd.
Eenadu Urban Co operative Bank
Goa Urban Co-operative Bank
Gopinath Patil Parsik Janata Sahakari Bank
Greater Bombay Co-operative Bank
Indian Mercantile Co-operative Bank
Kalupur Commercial Coop. Bank
Jalgaon Janata Sahakari Bank
Janakalyan Sahakari Bank
Janalaxmi Co-operative Bank
Janata Sahakari Bank
Janaseva Sahakari Bank Ltd.,Pune
Junagadh Commercial Co-operative Bank
Kallappanna Awade Ichalkaranji Janata Sahakari Bank
Kalyan Janata Sahakari Bank
Karad Urban Co-operative Bank
Khamgaon Urban Co-operative Bank
Mahanagar Co-operative Bank
Mattancherry Sarvajanik Co-operative Bank
Mapusa Urban Co-operative Bank of Goa
Mehsana Urban Co-Op Bank
Muneshwra swamy BANK
Nagar Urban Co-operative Bank
Nagpur Nagrik Sahakari Bank
Nasik Merchant’s Co-operative Bank
North 24 Parganas Co-Operative(Bank) Society Private Limited;
New India Co-operative Bank
Nutan Nagarik Sahakari Bank
NKGSB Co-operative Bank
Rajdhani Nagar Sahkari Bank
Rupee Co-operative Bank
Pravara Sahakari Bank
Punjab & Maharashtra Co-operative Bank
Rajkot Nagrik Sahakari Bank
Rajkot District Co-Op Bank
Sangli Urban Co-operative Bank
Saraswat Co-operative Bank
Sardar Bhiladwala Pardi Peoples Coop Bank
Shamrao Vithal Co-operative Bank
Shikshak Sahakari Bank
Solapur Janata Sahakari Bank
Surat Peoples Coop Bank
Surat District Coop Bank
Thane Bharat Sahakari Bank
The Bangalore City Co-Op Bank Ltd
THE Jaynagar Mozilpur People's Co-operative Bank Ltd.
The Kapole Co-operative Bank
The Surat District Co-Op Bank Ltd
THE SUTEX CO-OP. BANK LTD.
TJSB Sahakari Bank
The Varachha Co-op Bank Ltd., Surat
Zoroastrian Co-operative Bank
Rohit Kataria Co-operative Bank
Sangli District Primary Teachers Bank Ltd, Sangli
Chartered Mercantile M.B. Ltd, Lucknow, U.P.
Lic of india staff co operative bank. H.O Pattom Thiruvananthapuram
The Bardoli Nagarik Sahakari Bank Ltd
Malad sahkari Bank Ltd
Cosmos Co-operative Bank Ltd
Foreign Banks[edit]
Foreign Banks with branches in India[edit]
List of banks which are incorporated outside India and are operating branches in India:
Australian Banks
Australia and New Zealand Banking Group
National Australia Bank
Westpac Banking Corporation
Bahraini Banks
Bank of Bahrain and Kuwait
Bangladeshi banks
AB Bank
Sonali Bank
Belgian Bank
Antwerp Diamond Bank
Canadian Bank
Bank of Nova Scotia
Chinese Bank
Industrial & Commercial Bank of China
Bank of China
French Banks
BNP Paribas
Credit Agricole
Societe Generale
German Banks
Deutsche Bank
Indonesian Bank
Bank Internasional Indonesia
Iran Bank
Pasargad Bank
Japanese Banks
Mizuho Corporate Bank
Sumitomo Mitsui Banking
Bank of Tokyo-Mitsubishi
Mauritian Bank
State Bank of Mauritius
Dutch Bank
Rabobank
Qatari Bank
Doha Bank
Qatar National Bank
Russian Banks
Sberbank
VTB
Singaporean Banks
DBS Bank
United Overseas Bank
South African Bank
FirstRand Bank
South Korean Banks
Shinhan Bank
Woori Bank
Sri Lankan Bank
Bank of Ceylon
Swiss Banks
Credit Suisse
UBS AG
Taiwanese Bank
Chinatrust Commercial Bank
Thai Bank
Krung Thai Bank
UAE Banks
Abu Dhabi Commercial Bank
Mashreq Bank
UK Banks
HSBC (as HSBC Bank India)
Barclays Bank
Standard Chartered Bank
US Banks
Bank of America
Citibank
J.P. Morgan Chase Bank
Goldman Sachs
Foreign Banks with representative offices in India[edit]
List of Foreign Banks with representative offices in India (as of 31 January 2015):
Austrian Bank
Raiffeisen Zentralbank
Belgian Bank
KBC Bank
Canadian Banks
Royal Bank of Canada
Toronto Dominion Bank
French Banks
Credit Industriel et Commercial
Natixis
German Banks
Commerzbank
DZ Bank
KfW
Landesbank Baden-Württemberg
Italian Banks
Banca Monte dei Paschi di Siena
Banca Popolare di Milano
Banca Popolare di Vicenza
Intesa Sanpaolo
UBI Banca
Malaysian Bank
CIMB
Nepalese Bank
Everest Bank
Norwegian bank
DNB ASA
Portuguese Bank
Caixa Geral de Depositos
Russian Banks
Gazprombank
Promsvyazbank
Vnesheconombank
South Korean Banks
Industrial Bank of Korea
Kookmin Bank
Korea Exchange Bank
Spanish Banks
Banco de Sabadell
Banco Bilbao Vizcaya Argentaria
Caixabank
Sri Lankan Bank
Hatton National Bank
Swedish Bank
Skandinaviska Enskilda Banken
Swiss Bank
Zurich Cantonal Bank
Taiwanese Banks
Bank of Taiwan
Mega International Commercial Bank
Turkish Bank
Bank Asya
UAE Banks
Emirates NBD
First Gulf Bank
UK Bank
Duncan Lawrie
US Banks
Bank of New York Mellon
Singapore Banks
Development Bank of Singapore
Local Area Banks[edit]
Coastal Local Area Bank Limited
Krishna Bhima Samruddhi Local Area Bank Limited
Subhadra Local Area Bank Limited
Payments Banks[edit]
Airtel Payments Bank Limited
Fino Payments Bank Limited
India Post Payments Bank
Aditya Birla Idea Payments bank
NSDL Payments Bank
Paytm Payments Bank
Private-Sector Banks[edit]
Bank Name
Established
Headquarter
Branches
Revenues
Total Assets
Ref/Notes
Axis Bank 1993 Mumbai, Maharashtra 3,304 ₹414.0925 billion (US$6.0 billion) ₹6.01467 trillion (US$88 billion)
Bandhan Bank 2014 Kolkata, West Bengal 840 ₹4,320.12 crore (US$630 million) ₹302.36 billion (US$4.4 billion)
Catholic Syrian Bank 1920 Thrissur, Kerala 426 ₹1,617.5 crore (US$240 million) ₹162.2324 billion (US$2.4 billion)
City Union Bank 1904 Thanjavur, Tamil Nadu ₹29.44 billion (US$430 million) ₹312.52 billion (US$4.5 billion)
DCB Bank 1930 Mumbai, Maharashtra ₹20.76 billion (US$300 million) ₹240.46 billion (US$3.5 billion)
Dhanlaxmi Bank 1927 Thrissur, Kerala ₹12 billion (US$170 million) ₹123.33 billion (US$1.8 billion)
Federal Bank 1931-49 Kochi, Kerala 1,252 ₹97.59 billion (US$1.4 billion) ₹1.149 trillion (US$17 billion)
HDFC Bank 1994 Mumbai, Maharashtra 4,715 ₹816.02 billion (US$12 billion) ₹8.638 trillion (US$130 billion)
ICICI Bank 1994 Mumbai, Maharashtra 4,867 ₹736.60 billion (US$11 billion) ₹11.242 trillion (US$160 billion) [1]
IndusInd Bank 1994 Mumbai, Maharashtra 1,004 ₹185.77 billion (US$2.7 billion) ₹1.786 trillion (US$26 billion)
IDFC Bank 2015 Mumbai, Maharashtra 100+ ₹85.327 billion (US$1.2 billion) ₹1.1216 trillion (US$16 billion)
Karnataka Bank 1924 Mangaluru, Karnataka 807 ₹51.85 billion (US$750 million) ₹641.26 billion (US$9.3 billion)
Karur Vysya Bank 1916 Karur, Tamil Nadu 668 ₹54.43 billion (US$790 million) ₹576.63 billion (US$8.4 billion)
Kotak Mahindra Bank 2003 Mumbai, Maharashtra 1,369 ₹211.76 billion (US$3.1 billion) ₹2.146 trillion (US$31 billion)
Lakshmi Vilas Bank 1926 Chennai, Tamil Nadu 565 ₹25.68 billion (US$370 million) ₹287.32 billion (US$4.2 billion)
Nainital Bank 1922 Nainital, Uttarakhand 135 ₹6.12 billion (US$89 million) ₹7.7 billion (US$110 million)
RBL Bank 1943 Mumbai, Maharashtra 342 ₹44.68 billion (US$650 million) ₹486.74 billion (US$7.1 billion)
South Indian Bank 1929 Thrissur, Kerala 852 ₹65.62 billion (US$950 million) ₹743.12 billion (US$11 billion)
Tamilnad Mercantile Bank Limited 1921 Thoothukudi, Tamil Nadu ₹38.11 billion (US$550 million) ₹32.24 billion (US$470 million)
U.P Agro Corporation Ban 2013 Mainpuri, Uttar Pradesh 11 (+19)
Yes Bank 2004 Mumbai, Maharashtra 1,050 ₹205.81 billion (US$3.0 billion) ₹2.15 trillion (US$31 billion)
Public-Sector Bank[edit]
Bank Name
Established
Headquarter
Branches
Revenues
Total Assets
Ref/Notes
Allahabad Bank 1865 Kolkata, West Bengal 3,245 ₹188.85 billion (US$2.7 billion) ₹2,364.60 billion (US$34 billion)
Andhra Bank 1923 Hyderabad, Telangana 2,803 ₹180.27 billion (US$2.6 billion) ₹2,221.26 billion (US$32 billion)
Bank of Baroda 1908 Vadodara, Gujarat 5,481 ₹422 billion (US$6.1 billion) ₹6,949 billion (US$100 billion)
Bank of India 1906 Mumbai, Maharashtra 5,100 ₹418 billion (US$6.1 billion) ₹6,100 billion (US$89 billion)
Bank of Maharashtra 1935 Pune, Maharashtra 1,897 ₹130.53 billion (US$1.9 billion) ₹1,610 billion (US$23 billion)
Canara Bank 1906 Bengaluru, Karnataka 6,639 ₹489.4 billion (US$7.1 billion) ₹5,530 billion (US$80 billion)
Central Bank of India 1911 Mumbai, Maharashtra 4,715 ₹259 billion (US$3.8 billion) ₹3,055 billion (US$44 billion)
Corporation Bank 1906 Mangalore, Karnataka 2,440 ₹194.12 billion (US$2.8 billion) ₹2,349 billion (US$34 billion)
Dena Bank 1938 Mumbai, Maharashtra 1,874 ₹106.45 billion (US$1.5 billion) ₹1,335 billion (US$19 billion)
Indian Bank 1907 Chennai, Tamil Nadu 2,896 ₹216.9 billion (US$3.2 billion) ₹3,648 billion (US$53 billion)
Indian Overseas Bank 1937 Chennai, Tamil Nadu 3,400 ₹235.2 billion (US$3.4 billion) ₹2,745 billion (US$40 billion)
IDBI Bank 1964 Mumbai, Maharashtra 1,995 ₹280.43 billion (US$4.1 billion) ₹3,744 billion (US$54 billion)
Oriental Bank of Commerce 1943 Gurgaon, Haryana 1,092 ₹200.6 billion (US$2.9 billion) ₹2,375.4 billion (US$35 billion)
Punjab and Sind Bank 1908 New Delhi 1,554 ₹87.44 billion (US$1.3 billion) ₹1,025.8 billion (US$15 billion)
Punjab National Bank 1894 New Delhi 6,937 ₹474.25 billion (US$6.9 billion) ₹6,674 billion (US$97 billion)
State Bank of India 1955 Mumbai, Maharashtra 17,170 ₹2.11 trillion (US$31 billion) ₹34.45 trillion (US$500 billion) [2]
Syndicate Bank 1925 Manipal, Karnataka 3500+ ₹69.13 billion (US$1.0 billion) ₹2,990 billion (US$44 billion)
UCO Bank 1943 Kolkata, West Bengal 4000+ ₹185.61 billion (US$2.7 billion) ₹2,448.9 billion (US$36 billion)
Union Bank of India 1919 Mumbai, Maharashtra 4,214 ₹322 billion (US$4.7 billion) ₹4,047 billion (US$59 billion)
United Bank of India 1950 Kolkata, West Bengal 2,054 ₹99.37 billion (US$1.4 billion) ₹1,230 billion (US$18 billion)
Vijaya Bank 1931 Bengaluru, Karnataka 2,031 ₹123.8 billion (US$1.8 billion) ₹1,549 billion (US$23 billion)
Regional Rural Banks (RRBs)[edit]
List of Regional Rural Banks in India:
Andhra Pradesh
Andhra Pragathi Grameena Bank
Chaitanya Godavari Grameena Bank
Saptagiri Grameena Bank
Assam
Assam Gramin Vikash Bank
Langpi Dehangi Rural Bank
Arunachal Pradesh
Arunachal Pradesh Rural Bank
Bihar
Uttar Bihar Gramin Bank
Madhya Bihar Gramin Bank
Bihar Gramin Bank
Chhattisgarh
Chhattisgarh Rajya Gramin Bank
Gujarat
Dena Gujarat Gramin Bank
Baroda Gujarat Gramin Bank
Saurashtra Gramin Bank
Haryana
Sarva Haryana Gramin Bank
Himachal Pradesh
Himachal Pradesh Gramin Bank
Jharkhand
Jharkhand Gramin Bank
Vananchal Gramin Bank
Jammu & Kashmir
Jammu And Kashmir Grameen Bank
Ellaquai Dehati Bank
Karnataka
Kaveri Grameena Bank
Karnataka Vikas Grameena Bank
Pragathi Krishna Gramin Bank
Kerala
Kerala Gramin Bank
Madhya Pradesh
Narmada Jhabua Gramin Bank
Central Madhya Pradesh Gramin Bank
Madhyanchal Gramin Bank
Maharashtra
Maharashtra Gramin Bank
Vidarbha Kokan Gramin Bank
Manipur
Manipur Rural Bank
Meghalaya
Meghalaya Rural Bank
Mizoram
Mizoram Rural Bank
Nagaland
Nagaland Rural Bank
Odisha
Odisha Gramya Bank
Utkal Grameen Bank
Punjab
Punjab Gramin Bank
Malwa Gramin Bank
Sutlej Gramin Bank
Puducherry
Puduvai Bharathiar Grama Bank
Rajasthan
Baroda Rajasthan Kshetriya Gramin Bank
Marudhara Rajasthan Gramin Bank
Tamil Nadu
Pandyan Grama Bank
Pallavan Grama Bank
Telangana
Andhra Pradesh Grameena Vikas Bank
Telangana Grameena Bank
Tripur
Tripura Gramin Bank
Uttar Pradesh
Sarva UP Gramin Bank
Prathama Bank
Allahabad UP Gramin Bank
Baroda UP Gramin Bank
Gramin Bank Of Aryavrat
Kashi Gomti Samyukt Gramin Bank
Purvanchal Bank
Uttarakhand
Uttarakhand Gramin Bank
West Bengal
Bangiya Gramin Vikash Bank
Paschim Banga Gramin Bank
Uttarbanga Kshetriya Gramin Bank
Small Finance Banks[edit]
AU Small Finance Bank
Capital Small Finance Bank
Equitas Small Finance Bank
ESAF Small Finance Bank
Fincare Small Finance Bank
Janalakshmi Small Finance Bank
North East Small Finance Bank
Suryoday Small Finance Bank
Ujjivan Small Finance Bank
Utkarsh Small Finance Bank
See also[edit]
India portal
Lists portal
State Bank of India
Reserve Bank of India
Banking in India
References[edit]
Jump up ^ "ICICI Bank About Us".
Jump up ^ "SBi annual report 2016-17" (PDF).
Adityabirla payments bank launches operationsadityabirla payments bank launches operations
External links[edit]
"Banks in India". Reserve Bank of India.
Retrieved from "https://en.wikipedia.org/w/index.php?title=List_of_banks_in_India&oldid=854596513"
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