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ATP synthase
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ATP Synthase
Molecular model of ATP synthase determined by X-ray crystallography. Stator is not shown here.
Identifiers
EC number
3.6.3.14
CAS number
9000-83-3
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BRENDA entry
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KEGG entry
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ATP synthase is an enzyme that creates the energy storage molecule adenosine triphosphate (ATP). ATP is the most commonly used "energy currency" of cells for most organisms. It is formed from adenosine diphosphate (ADP) and inorganic phosphate (Pi). The overall reaction catalyzed by ATP synthase is:
ADP + Pi + H+out ⇌ ATP + H2O + H+in
The formation of ATP from ADP and Pi is energetically unfavorable and would normally proceed in the reverse direction. In order to drive this reaction forward, ATPase couples ATP synthesis during cellular respiration to an electrochemical gradient created by the difference in proton (H+) concentration across the mitochondrial membrane in eukaryotes or the plasma membrane in bacteria. During photosynthesis in plants, ATP is synthesized by ATPase using a proton gradient created in the thylakoid lumen through the thylakoid membrane and into the chloroplast stroma.
ATP synthase consists of two main subunits, FO and F1, which has a rotational motor mechanism allowing for ATP production.[1][2] Because of its rotating subunit ATP Synthase is a molecular machine.
Contents
[hide]
1 Nomenclature
2 Structure and function
2.1 F1 region
2.2 FO region
3 Binding model
4 Physiological role
5 Evolution
6 In different species
6.1 E. coli
6.2 Yeast
6.3 Plant
6.4 Bovine
6.5 Human
7 See also
8 References
9 Further reading
10 External links
Nomenclature[edit]
The F1 fraction derives its name from the term "Fraction 1" and FO (written as a subscript letter "o", not "zero") derives its name from being the binding fraction for oligomycin, a type of naturally-derived antibiotic that is able to inhibit the FO unit of ATP synthase.[3][4] These functional regions consist of different protein subunits — refer to tables.
Structure and function[edit]
Bovine mitochondrial ATP synthase. The FO, F1, axle, and stator regions are color coded magenta, green, orange, and cyan respectively.[5][6]
Simplified model of FOF1-ATPase alias ATP synthase of E. coli. Subunits of the enzyme are labeled accordingly.
Rotation engine of ATP synthase.
Located within the thylakoid membrane and the inner mitochondrial membrane, ATP synthase consists of two regions FO and F1. FO causes rotation of F1 and is made of c-ring and subunits a, b, d, F6. F1 is made of α , β , γ , δ {\displaystyle \alpha ,\beta ,\gamma ,\delta } subunits. F1 has a water soluble par that can hydrolyze ATP. FO on the other hand has mainly hydrophobic regions. FO F1 creates a pathway for protons movement across the membrane.[7]
F1 region[edit]
The F1 portion of ATP synthase is hydrophilic and responsible for hydrolyzing ATP. Subunits α {\displaystyle \alpha } and β {\displaystyle \beta } make a hexamer with 6 binding sites. Three of them are catalytically inactive and they bind ADP.
Other three subunits catalyze the ATP synthesis. The other F1 subunits γ , δ , ϵ {\displaystyle \gamma ,\delta ,\epsilon } are a part of a rotational motor mechanism. γ {\displaystyle \gamma } subunit allows β {\displaystyle \beta } to go though conformational changes, i.e closed, half open and open states allows for ATP to be bound and released once synthesized. The F1 particle is large and can be seen in the transmission electron microscope by negative staining.[8] These are particles of 9 nm diameter that pepper the inner mitochondrial membrane.
F1 - Subunits
Subunit
Human Gene
alpha ATP5A1, ATPAF2
beta ATP5B, ATPAF1, C16orf7
gamma ATP5C1
delta ATP5D
epsilon ATP5E
FO region[edit]
FO subunit F6 from the peripheral stalk region of ATP synthase.[9]
Fo is a water insoluble protein with eight subunits and transmembrane ring. The ring has a tetramer shape with protein helix loop helix that goes though conformational change when protonated and deprotonated allowing to push neighboring subunits to rotate causing the spinning of FO which then affects conformation of F1 also, resulting on switching of states of alpha and beta subunits. The FO region of ATP synthase is a proton pore that is embedded in the mitochondrial membrane. It consists of three main subunits a, b, and c, and (in humans) six additional subunits, d, e, f, g, F6, and 8 (or A6L). An atomic model for the dimeric yeast FO region was determined by cryo-EM at an overall resolution of 3.6 Å [10]
FO-Main subunits
Subunit
Human Gene
a ATP6
b ATP5F1
c ATP5G1, ATP5G2, ATP5G3
Binding model[edit]
Mechanism of ATP synthase. ADP and Pi (pink) shown being combined into ATP (red), and the rotating γ (gamma) subunit in black causing conformation.
Depiction of ATP synthase using the chemiosmotic proton gradient to power ATP synthesis through oxidative phosphorylation.
In the 1960s through the 1970s, Paul Boyer, a UCLA Professor, developed the binding change, or flip-flop, mechanism theory, which postulated that ATP synthesis is dependent on a conformational change in ATP synthase generated by rotation of the gamma subunit. The research group of John E. Walker, then at the MRC Laboratory of Molecular Biology in Cambridge, crystallized the F1 catalytic-domain of ATP synthase. The structure, at the time the largest asymmetric protein structure known, indicated that Boyer's rotary-catalysis model was, in essence, correct. For elucidating this, Boyer and Walker shared half of the 1997 Nobel Prize in Chemistry.
The crystal structure of the F1 showed alternating alpha and beta subunits (3 of each), arranged like segments of an orange around a rotating asymmetrical gamma subunit. According to the current model of ATP synthesis (known as the alternating catalytic model), the transmembrane potential created by (H+) proton cations supplied by the electron transport chain, drives the (H+) proton cations from the intermembrane space through the membrane via the FO region of ATP synthase. A portion of the FO (the ring of c-subunits) rotates as the protons pass through the membrane. The c-ring is tightly attached to the asymmetric central stalk (consisting primarily of the gamma subunit), causing it to rotate within the alpha3beta3 of F1 causing the 3 catalytic nucleotide binding sites to go through a series of conformational changes that leads to ATP synthesis. The major F1 subunits are prevented from rotating in sympathy with the central stalk rotor by a peripheral stalk that joins the alpha3beta3 to the non-rotating portion of FO. The structure of the intact ATP synthase is currently known at low-resolution from electron cryo-microscopy (cryo-EM) studies of the complex. The cryo-EM model of ATP synthase suggests that the peripheral stalk is a flexible structure that wraps around the complex as it joins F1 to FO. Under the right conditions, the enzyme reaction can also be carried out in reverse, with ATP hydrolysis driving proton pumping across the membrane.
The binding change mechanism involves the active site of a β subunit's cycling between three states.[11] In the "loose" state, ADP and phosphate enter the active site; in the adjacent diagram, this is shown in pink. The enzyme then undergoes a change in shape and forces these molecules together, with the active site in the resulting "tight" state (shown in red) binding the newly produced ATP molecule with very high affinity. Finally, the active site cycles back to the open state (orange), releasing ATP and binding more ADP and phosphate, ready for the next cycle of ATP production.[12]
Physiological role[edit]
Like other enzymes, the activity of F1FO ATP synthase is reversible. Large-enough quantities of ATP cause it to create a transmembrane proton gradient, this is used by fermenting bacteria that do not have an electron transport chain, but rather hydrolyze ATP to make a proton gradient, which they use to drive flagella and the transport of nutrients into the cell.
In respiring bacteria under physiological conditions, ATP synthase, in general, runs in the opposite direction, creating ATP while using the proton motive force created by the electron transport chain as a source of energy. The overall process of creating energy in this fashion is termed oxidative phosphorylation. The same process takes place in the mitochondria, where ATP synthase is located in the inner mitochondrial membrane and the F1-part projects into mitochondrial matrix. The consumption of ATP by ATP-synthase pumps proton cations into the matrix.
Evolution[edit]
The evolution of ATP synthase is thought to have been modular whereby two functionally independent subunits became associated and gained new functionality.[13][14] This association appears to have occurred early in evolutionary history, because essentially the same structure and activity of ATP synthase enzymes are present in all kingdoms of life.[13] The F-ATP synthase displays high functional and mechanistic similarity to the V-ATPase.[15] However, whereas the F-ATP synthase generates ATP by utilising a proton gradient, the V-ATPase generates a proton gradient at the expense of ATP, generating pH values of as low as 1.[16]
The F1 region also shows significant similarity to hexameric DNA helicases, and the FO region shows some similarity to H+
-powered flagellar motor complexes.[15] The α3β3 hexamer of the F1 region shows significant structural similarity to hexameric DNA helicases; both form a ring with 3-fold rotational symmetry with a central pore. Both have roles dependent on the relative rotation of a macromolecule within the pore; the DNA helicases use the helical shape of DNA to drive their motion along the DNA molecule and to detect supercoiling, whereas the α3β3 hexamer uses the conformational changes through the rotation of the γ subunit to drive an enzymatic reaction.[17]
The H+
motor of the FO particle shows great functional similarity to the H+
motors that drive flagella.[15] Both feature a ring of many small alpha-helical proteins that rotate relative to nearby stationary proteins, using a H+
potential gradient as an energy source. This link is tenuous, however, as the overall structure of flagellar motors is far more complex than that of the FO particle and the ring with about 30 rotating proteins is far larger than the 10, 11, or 14 helical proteins in the FO complex.
The modular evolution theory for the origin of ATP synthase suggests that two subunits with independent function, a DNA helicase with ATPase activity and a H+
motor, were able to bind, and the rotation of the motor drove the ATPase activity of the helicase in reverse.[13][17] This complex then evolved greater efficiency and eventually developed into today's intricate ATP synthases. Alternatively, the DNA helicase/H+
motor complex may have had H+
pump activity with the ATPase activity of the helicase driving the H+
motor in reverse.[13] This may have evolved to carry out the reverse reaction and act as an ATP synthase.[14][18][19]
In different species[edit]
E. coli[edit]
E. coli ATP synthase is the simplest known form of ATP synthase, with 8 different subunit types.[20]
Yeast[edit]
Yeast ATP synthase is one of the best-studied eukaryotic ATP synthases; and five F1, eight FO subunits, and seven associated proteins have been identified.[7] Most of these proteins have homologues in other eukaryotes.[21][22][23]
Plant[edit]
In plants, ATP synthase is also present in chloroplasts (CF1FO-ATP synthase). The enzyme is integrated into thylakoid membrane; the CF1-part sticks into stroma, where dark reactions of photosynthesis (also called the light-independent reactions or the Calvin cycle) and ATP synthesis take place. The overall structure and the catalytic mechanism of the chloroplast ATP synthase are almost the same as those of the mitochondrial enzyme. However, in chloroplasts, the proton motive force is generated not by respiratory electron transport chain but by primary photosynthetic proteins.
Bovine[edit]
The ATP synthase isolated from bovine heart mitochondria (Bos taurus) is, in terms of biochemistry and structure, the best-characterized ATP synthase. Beef heart is used as a source for the enzyme because of the high concentration of mitochondria in cardiac muscle.[24][25][26]
Human[edit]
The following is a list of humans genes that encode components of ATP synthases:
ATP5A1, ATP5AL1
ATP5B, ATP5BL1
ATP5C2, ATP5D, ATP5E, ATP5F1, ATP5G1, ATP5G2, ATP5G3, ATP5H, ATP5HP1, ATP5I, ATP5J, ATP5J2, ATP5L, ATP5L2, ATP5O, ATP5S
ATP6, ATP6AP1, ATP6AP2
ATPSBL1, ATPSBL2
MT-ATP6, MT-ATP8
See also[edit]
ATP10 protein required for the assembly of the FO sector of the mitochondrial ATPase complex.
Chloroplast
Electron transfer chain
Flavoprotein
Mitochondrion
Oxidative phosphorylation
P-ATPase
Proton pump
Rotating locomotion in living systems
Transmembrane ATPase
V-ATPase
References[edit]
Jump up ^ Okuno D, Iino R, Noji H (April 2011). "Rotation and structure of FOF1-ATP synthase". Journal of Biochemistry. 149 (6): 655–64. doi:10.1093/jb/mvr049. PMID 21524994.
Jump up ^ Junge W, Nelson N (June 2015). "ATP synthase". Annual Review of Biochemistry. 84: 631–57. doi:10.1146/annurev-biochem-060614-034124. PMID 25839341.
Jump up ^ Kagawa Y, Racker E (May 1966). "Partial resolution of the enzymes catalyzing oxidative phosphorylation. 8. Properties of a factor conferring oligomycin sensitivity on mitochondrial adenosine triphosphatase". The Journal of Biological Chemistry. 241 (10): 2461–6. PMID 4223640.
Jump up ^ Mccarty RE (November 1992). "A plant biochemist's view of H+
-ATPases and ATP synthases". The Journal of Experimental Biology. 172 (Pt 1): 431–441. PMID 9874753.
Jump up ^ PDB: 5ARA; Zhou A, Rohou A, Schep DG, Bason JV, Montgomery MG, Walker JE, Grigorieff N, Rubinstein JL (October 2015). "Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM". eLife. 4: e10180. doi:10.7554/eLife.10180. PMC 4718723  . PMID 26439008.
Jump up ^ Goodsell D (December 2005). "ATP Synthase". Molecule of the Month. RCSB PDB. doi:10.2210/rcsb_pdb/mom_2005_12.
^ Jump up to: a b Velours J, Paumard P, Soubannier V, Spannagel C, Vaillier J, Arselin G, Graves PV (May 2000). "Organisation of the yeast ATP synthase F(0):a study based on cysteine mutants, thiol modification and cross-linking reagents". Biochimica et Biophysica Acta. 1458 (2–3): 443–56. doi:10.1016/S0005-2728(00)00093-1. PMID 10838057.
Jump up ^ Fernandez Moran H, Oda T, Blair PV, Green DE (July 1964). "A macromolecular repeating unit of mitochondrial structure and function. Correlated electron microscopic and biochemical studies of isolated mitochondria and submitochondrial particles of beef heart muscle". The Journal of Cell Biology. 22 (1): 63–100. doi:10.1083/jcb.22.1.63. PMC 2106494  . PMID 14195622.
Jump up ^ PDB: 1VZS; Carbajo RJ, Silvester JA, Runswick MJ, Walker JE, Neuhaus D (2004). "Solution structure of subunit F(6) from the peripheral stalk region of ATP synthase from bovine heart mitochondria". Journal of Molecular Biology. 342 (2): 593–603. doi:10.1016/j.jmb.2004.07.013. PMID 15327958.
Jump up ^ Guo H, Bueler SA, Rubinstein JL (Nov 2017). "Atomic model for the dimeric FO region of mitochondrial ATP synthase". Science. 358 (6365): 936–40. doi:10.1126/science.aao4815. PMID 29074581.
Jump up ^ Gresser MJ, Myers JA, Boyer PD (October 1982). "Catalytic site cooperativity of beef heart mitochondrial F1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model". The Journal of Biological Chemistry. 257 (20): 12030–8. PMID 6214554.
Jump up ^ Nakamoto RK, Baylis Scanlon JA, Al-Shawi MK (August 2008). "The rotary mechanism of the ATP synthase". Archives of Biochemistry and Biophysics. 476 (1): 43–50. doi:10.1016/j.abb.2008.05.004. PMC 2581510  . PMID 18515057.
^ Jump up to: a b c d Doering C, Ermentrout B, Oster G (December 1995). "Rotary DNA motors". Biophysical Journal. 69 (6): 2256–67. Bibcode:1995BpJ....69.2256D. doi:10.1016/S0006-3495(95)80096-2. PMC 1236464  . PMID 8599633.
^ Jump up to: a b Crofts A. "Lecture 10:ATP synthase". Life Sciences at the University of Illinois at Urbana-Champaign.
^ Jump up to: a b c "ATP Synthase". InterPro Database.
Jump up ^ Kim MS, Jang J, Ab Rahman NB, Pethe K, Berry EA, Huang LS (June 2015). "Isolation and Characterization of a Hybrid Respiratory Supercomplex Consisting of Mycobacterium tuberculosis Cytochrome bcc and Mycobacterium smegmatis Cytochrome aa3". The Journal of Biological Chemistry. 290 (23): 14350–60. doi:10.1074/jbc.m114.624312. PMC 4505504  . PMID 25861988.
^ Jump up to: a b Martinez LO, Jacquet S, Esteve JP, Rolland C, Cabezón E, Champagne E, Pineau T, Georgeaud V, Walker JE, Tercé F, Collet X, Perret B, Barbaras R (January 2003). "Ectopic beta-chain of ATP synthase is an apolipoprotein A-I receptor in hepatic HDL endocytosis". Nature. 421 (6918): 75–9. Bibcode:2003Natur.421...75M. doi:10.1038/nature01250. PMID 12511957.
Jump up ^ Cross RL, Taiz L (January 1990). "Gene duplication as a means for altering H+/ATP ratios during the evolution of FOF1 ATPases and synthases". FEBS Letters. 259 (2): 227–9. doi:10.1016/0014-5793(90)80014-a. PMID 2136729.
Jump up ^ Cross RL, Müller V (October 2004). "The evolution of A-, F-, and V-type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio". FEBS Letters. 576 (1–2): 1–4. doi:10.1016/j.febslet.2004.08.065. PMID 15473999.
Jump up ^ Ahmad Z, Okafor F, Laughlin TF. "Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase". Journal of Amino Acids. 2011: 785741. doi:10.4061/2011/785741. PMID 22312470.
Jump up ^ Devenish RJ, Prescott M, Roucou X, Nagley P (May 2000). "Insights into ATP synthase assembly and function through the molecular genetic manipulation of subunits of the yeast mitochondrial enzyme complex". Biochimica et Biophysica Acta. 1458 (2–3): 428–42. doi:10.1016/S0005-2728(00)00092-X. PMID 10838056.
Jump up ^ Kabaleeswaran V, Puri N, Walker JE, Leslie AG, Mueller DM (November 2006). "Novel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase". The EMBO Journal. 25 (22): 5433–42. doi:10.1038/sj.emboj.7601410. PMID 17082766.
Jump up ^ Stock D, Leslie AG, Walker JE (November 1999). "Molecular architecture of the rotary motor in ATP synthase". Science. 286 (5445): 1700–5. PMID 10576729.
Jump up ^ Abrahams JP, Leslie AG, Lutter R, Walker JE (August 1994). "Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria". Nature. 370 (6491): 621–8. doi:10.1038/370621a0. PMID 8065448.
Jump up ^ Gibbons C, Montgomery MG, Leslie AG, Walker JE (November 2000). "The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution". Nature Structural Biology. 7 (11): 1055–61. doi:10.1038/80981. PMID 11062563.
Jump up ^ Menz RI, Walker JE, Leslie AG (August 2001). "Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis". Cell. 106 (3): 331–41. PMID 11509182.
Further reading[edit]
Nick Lane: The Vital Question - Energy, Evolution, and the Origins of Complex Life, Ww Norton, 2015-07-20, ISBN 978-0393088816 (Link points to Figure 10 showing model of ATP synthase)
External links[edit]
Boris A. Feniouk: "ATP synthase — a splendid molecular machine"
Well illustrated ATP synthase lecture by Antony Crofts of the University of Illinois at Urbana-Champaign.
Proton and Sodium translocating F-type, V-type and A-type ATPases in OPM database
The Nobel Prize in Chemistry 1997 to Paul D. Boyer and John E. Walker for the enzymatic mechanism of synthesis of ATP; and to Jens C. Skou, for discovery of an ion-transporting enzyme, Na+
, K+
-ATPase.
Harvard Multimedia Production Site — Videos — ATP synthesis animation
David Goodsell: "ATP Synthase- Molecule of the Month"
[show]
v
t
e
Membrane transport protein: ion pumps, ATPases / ATP synthase (TC 3A2-3A3)
F-, V-, and A-type ATPase (3.A.2)
H+ (F-type)
H+ transporting, mitochondrial: ATP5A1
ATP5B
ATP5C1
ATP5C2
ATP5D
ATP5E
ATP5F1
ATP5G1
ATP5G2
ATP5G3
ATP5H
ATP5I
ATP5J
ATP5J2
ATP5L
ATP5L2
ATP5O
ATP5S
H+ (V-type)
H+ transporting, lysosomal: ATP6AP1
ATP6AP2
ATP6V1A
ATP6V1B1
ATP6V1B2
ATP6V1C1
ATP6V1C2
ATP6V1D
ATP6V1E1
ATP6V1E2
ATP6V1F
ATP6V1G1
ATP6V1G2
ATP6V1G3
ATP6V1H
ATP6V0A1
ATP6V0A2
ATP6V0A4
ATP6V0B
ATP6V0C
ATP6V0D1
ATP6V0D2
ATP6V0E
ATP6V0E1
TCIRG1
A-ATPase
found in Archea
P-type ATPase (3.A.3)
3.A.3.1.1: Na+/K+ transporting: ATP1A1
ATP1A2
ATP1A3
ATP1A4
ATP1B1
ATP1B2
ATP1B3
ATP1B4
ATP1G1
3.A.3.1.2: H+/K+
H+/K+ exchanging: ATP4A
ATP4B
3.A.3.1.4: H+/K+ transporting, nongastric: ATP12A
3.A.3.2: Ca2+ (SERCA, PMCA, SPCA) / Ca2+ transporting: ATP2A1
ATP2A2
ATP2A3
ATP2B1
ATP2B2
ATP2B3
ATP2B4
ATP2C1
3.A.3.5: Cu2+ transporting: ATP7A
ATP7B
3.A.3.8.8: flippase: ATP8A2
Other/ungrouped:
Na+/K+ – H+
Mg2+ transporting: ATP3
Class I, type 8: ATP8A1
ATP8B1
ATP8B2
ATP8B3
ATP8B4
Class II, type 9: ATP9A
ATP9B
Class V, type 10: ATP10A
ATP10B
ATP10D
Class VI, type 11: ATP11A
ATP11B
ATP11C
type 13: ATP13A1
ATP13A2
ATP13A3
ATP13A4
ATP13A5
see also ATPase disorders
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MT-CO1
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ATP synthase
MT-ATP6
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tRNA
MT-TA
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MT-TY
see also mitochondrial diseases
[show]
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Hydrolases: acid anhydride hydrolases (EC 3.6)
3.6.1
Pyrophosphatase
Inorganic
Thiamine
Apyrase
Thiamine-triphosphatase
3.6.2
Adenylylsulfatase
Phosphoadenylylsulfatase
3.6.3-4: ATPase
3.6.3
Cu++ (3.6.3.4)
Menkes/ATP7A
Wilson/ATP7B
Ca+ (3.6.3.8)
SERCA
ATP2A1
ATP2A2
ATP2A3
Plasma membrane
ATP2B1
ATP2B2
ATP2B3
ATP2B4
SPCA
ATP2C1
ATP2C2
Na+/K+ (3.6.3.9)
ATP1A1
ATP1A2
ATP1A3
ATP1A4
ATP1B1
ATP1B2
ATP1B3
ATP1B4
H+/K+ (3.6.3.10)
ATP4A
Other P-type ATPase
ATP8B1
ATP10A
ATP11B
ATP12A
ATP13A2
ATP13A3
3.6.4
Dynein
Kinesin
Myosin
Katanin
3.6.5: GTPase
3.6.5.1: Heterotrimeric G protein
Gαs
Gαi
GNAI1
GNAI2
GNAI3
Gαq/11
GNAQ
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GNA12
GNA13
Transducin
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3.6.5.2: Small GTPase > Ras superfamily
Rho family of GTPases: Cdc42
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HRAS
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RGK
3.6.5.3: Protein-synthesizing GTPase
Prokaryotic
IF-2
EF-Tu
EF-G
Eukaryotic
3.6.5.5-6: Polymerization motors
Dynamin
Tubulin
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Molecular and Cellular Biology portal
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Humus
From Wikipedia, the free encyclopedia
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This article is about the organic matter in soil. For the food, see Hummus. For the band, see Humus (band).
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Humus has a characteristic black or dark brown color and is an accumulation of organic carbon. Besides the three major soil horizons of (A) surface/topsoil, (B) subsoil, and (C) substratum, some soils have an organic horizon (O) on the very surface. Hard bedrock (R) is not in a strict sense soil.
In soil science, humus (derived in 1790–1800 from the Latin humus for earth, ground[1]) denominates the fraction of soil organic matter that is amorphous and without the "cellular cake structure characteristic of plants, micro-organisms or animals."[2] Humus significantly affects the bulk density of soil and contributes to its retention of moisture and nutrients.
In agriculture, "humus" sometimes also is used to describe mature or natural compost extracted from a woodland or other spontaneous source for use as a soil conditioner.[3] It is also used to describe a topsoil horizon that contains organic matter (humus type,[4] humus form,[5] humus profile).[6]
Humus is the dark organic matter that forms in soil when dead plant and animal matter decays. Humus has many nutrients that improve the health of soil, nitrogen being the most important. The ratio of carbon to nitrogen (C:N) of humus is 10:1.
Contents
[hide]
1 Description
2 Humification
3 Stability
4 Horizons
5 Benefits of soil organic matter and humus
6 See also
7 References
8 External links
Description[edit]
It is difficult to define humus precisely because it is a very complex substance which is not fully understood. Humus is different from decomposing soil organic matter. The latter looks rough and has visible remains of the original plant or animal matter. Fully humified humus, on the contrary, has a uniformly dark, spongy, and jelly-like appearance, and is amorphous; it may gradually decompose over several years or persist for millennia.[7] It has no determinate shape, structure, or quality. However, when examined under a microscope, humus may reveal tiny plant, animal, or microbial remains that have been mechanically, but not chemically, degraded.[8] This suggests an ambiguous boundary between humus and soil organic matter. While distinct, humus is an integral part of soil organic matter.[9]
Humification[edit]
Microorganisms decompose a large portion of the soil organic matter into inorganic minerals that the roots of plants can absorb as nutrients. This process is termed "mineralization". In this process, nitrogen (nitrogen cycle) and the other nutrients (nutrient cycle) in the decomposed organic matter are recycled. Depending on the conditions in which the decomposition occurs, a fraction of the organic matter does not mineralize, and instead is transformed by a process called "humification" into concatenations of organic polymers. Because these organic polymers are resistant to the action of microorganisms, they are stable, and constitute humus. This stability implies that humus integrates into the permanent structure of the soil, thereby improving it.[10]
Humification can occur naturally in soil or artificially in the production of compost. Organic matter is humified by a combination of saprotrophic fungi, bacteria, microbes and animals such as earthworms, nematodes, protozoa, and arthropods.[11][better source needed] Plant remains, including those that animals digested and excreted, contain organic compounds: sugars, starches, proteins, carbohydrates, lignins, waxes, resins, and organic acids. Decay in the soil begins with the decomposition of sugars and starches from carbohydrates, which decompose easily as detritivores initially invade the dead plant organs, while the remaining cellulose and lignin decompose more slowly.[12] Simple proteins, organic acids, starches, and sugars decompose rapidly, while crude proteins, fats, waxes, and resins remain relatively unchanged for longer periods of time. Lignin, which is quickly transformed by white-rot fungi,[13] is one of the primary precursors of humus,[14] together with by-products of microbial[15] and animal[16] activity. The humus produced by humification is thus a mixture of compounds and complex biological chemicals of plant, animal, or microbial origin that has many functions and benefits in soil. Some judge earthworm humus (vermicompost) to be the optimal organic manure.[17]
Stability[edit]
Much of the humus in most soils has persisted for more than 100 years, rather than having been decomposed into CO2, and can be regarded as stable; this organic matter has been protected from decomposition by microbial or enzyme action because it is hidden (occluded) inside small aggregates of soil particles, or tightly sorbed or complexed) to clays.[18] Most humus that is not protected in this way is decomposed within 10 years and can be regarded as less stable or more labile. Stable humus contributes few plant-available nutrients in soil, but it helps maintain its physical structure.[19] A very stable form of humus is formed from the slow oxidation of soil carbon after the incorporation of finely powdered charcoal into the topsoil. This process is speculated to have been important in the formation of the very fertile Amazonian terra preta do Indio.[20]
Horizons[edit]
Humus has a characteristic black or dark brown color and is organic due to an accumulation of organic carbon. Soil scientists use the capital letters O, A, B, C, and E to identify the master horizons, and lowercase letters for distinctions of these horizons. Most soils have three major horizons: the surface horizon (A), the subsoil (B), and the substratum (C). Some soils have an organic horizon (O) on the surface, but this horizon can also be buried. The master horizon (E) is used for subsurface horizons that have significantly lost minerals (eluviation). Bedrock, which is not soil, uses the letter R.
Benefits of soil organic matter and humus[edit]
The importance of chemically stable humus is thought by some to be the fertility it provides to soils in both a physical and chemical sense,[21] though some agricultural experts put a greater focus on other features of it, such as its ability to suppress disease.[22] It helps the soil retain moisture[23] by increasing microporosity,[24] and encourages the formation of good soil structure.[25][26] The incorporation of oxygen into large organic molecular assemblages generates many active, negatively charged sites that bind to positively charged ions (cations) of plant nutrients, making them more available to the plant by way of ion exchange.[27] Humus allows soil organisms to feed and reproduce, and is often described as the "life-force" of the soil.[28][29]
The process that converts soil organic matter into humus feeds the population of microorganisms and other creatures in the soil, and thus maintains high and healthy levels of soil life.[28][29]
The rate at which soil organic matter is converted into humus promotes (when fast) or limits (when slow) the coexistence of plants, animals, and microorganisms in the soil.
Effective humus and stable humus are additional sources of nutrients for microbes: the former provides a readily available supply and the latter acts as a longeval storage reservoir.
Decomposition of dead plant material causes complex organic compounds to be slowly oxidized (lignin-like humus) or to decompose into simpler forms (sugars and amino sugars, and aliphatic and phenolic organic acids), which are further transformed into microbial biomass (microbial humus) or reorganized, and further oxidized, into humic assemblages (fulvic and humic acids), which bind to clay minerals and metal hydroxides. The ability of plants to absorb humic substances with their roots and metabolize them has been long debated. There is now a consensus that humus functions hormonally rather than simply nutritionally in plant physiology.[30][31]
Humus is a colloidal substance and increases the cation exchange capacity of soil, hence its ability to store nutrients by chelation. While these nutrient cations are available to plants, they are held in the soil and prevented from being leached by rain or irrigation.[27]
Humus can hold the equivalent of 80–90% of its weight in moisture, and therefore increases the soil's capacity to withstand drought.[32][33]
The biochemical structure of humus enables it to moderate, i. e. buffer, excessive acidic or alkaline soil conditions.[34]
During humification, microbes secrete sticky, gum-like mucilages; these contribute to the crumby structure (tilth) of the soil by adhering particles together and allowing greater aeration of the soil.[35] Toxic substances such as heavy metals and excess nutrients can be chelated, i. e., bound to the organic molecules of humus, and so prevented from leaching away.[36]
The dark, usually brown or black, color of humus helps to warm cold soils in Spring.
See also[edit]
Biochar
Biomass
Biotic material
Detritus
Glomalin
Humic acid
Immobilization (soil science)
Mineralization (soil science)
Mycorrhizal fungi and soil carbon storage
Organic matter
Plant litter
Soil horizon
Soil organic matter
Soil science
Terra preta
References[edit]
Jump up ^ "Humus." Dictionary.com Unabridged, version 1.1. Random House, Inc., 23 Sep 2008, in [1].
Jump up ^ Whitehead, D. C.; Tinsley, J. (1963). "The biochemistry of humus formation". Journal of the Science of Food and Agriculture. 14 (12): 849–857. doi:10.1002/jsfa.2740141201. Retrieved 26 July 2014.
Jump up ^ "Humus." Encyclopaedia Britannica. Encyclopaedia Britannica Online. Encyclopaedia Britannica Inc., 2011. Accessed 24 Nov 2011. <http://www.britannica.com/EBchecked/topic/276408/humus>.
Jump up ^ Chertov, O.G.; Kornarov, A.S.; Crocker, G.; Grace, P.; Klir, J.; Körschens, M.; Poulton, P.R.; Richter, D. (1997). "Simulating trends of soil organic carbon in seven long-term experiments using the SOMM model of the humus types". Geoderma. 81: 121–135. doi:10.1016/S0016-7061(97)00085-2.
Jump up ^ Baritz, R., 2003. Humus forms in forests of the northern German lowlands. Schweizerbart, Stuttgart, Germany, 145 pp.[2]
Jump up ^ Bunting, B.T.; Lundberg, J. (1995). "The humus profile-concept, class and reality". Geoderma. 40: 17–36. doi:10.1016/0016-7061(87)90011-5.
Jump up ^ Di Giovanni1, C.; Disnar, J.R.; Bichet, V.; Campy, M. (1998). "Sur la présence de matières organiques mésocénozoïques dans des humus actuels (bassin de Chaillexon, Doubs, France)". Comptes Rendus de l'Académie des Sciences, Série IIA. 326: 553–559. doi:10.1016/S1251-8050(98)80206-1.
Jump up ^ Nicolas Bernier and Jean-François Ponge (1994). "Humus form dynamics during the sylvogenetic cycle in a mountain spruce forest" (PDF). Soil Biology and Biochemistry. 26 (2): 183–220. doi:10.1016/0038-0717(94)90161-9.
Jump up ^ Humintech® | Definition Of Soil Organic Matter & Humic Acids Based Products
Jump up ^ Brady, N. C.; Weil, R. R. (1999). The nature and properties of soils. Upper Saddle River, N. J.: Prentice Hall, Inc.
Jump up ^ Soil biology
Jump up ^ Berg, B., McClaugherty, C., 2007. Plant litter: decomposition, humus formation, carbon sequestration, 2nd ed. Springer, 338 pp., ISBN 3-540-74922-5
Jump up ^ Levin, L.; Forchiassin, F.; Ramos, A.M. (2002). "Copper induction of lignin-modifying enzymes in the white-rot fungus Trametes trogii". Mycologia. 94: 377–383. doi:10.2307/3761771.
Jump up ^ González-Pérez, M.; Vidal Torrado, P.; Colnago, L.A.; Martin-Neto, L.; Otero, X.L.; Milori, D.M.B.P.; Haenel Gomes, F. (2008). "13C NMR and FTIR spectroscopy characterization of humic acids in spodosols under tropical rain forest in southeastern Brazil". Geoderma. 146: 425–433. doi:10.1016/j.geoderma.2008.06.018.
Jump up ^ Knicker, H.; Almendros, G.; González-Vila, F.J.; Lüdemann, H.D.; Martin, F. (1995). "13C and 15N NMR analysis of some fungal melanins in comparison with soil organic matter". Organic Geochemistry. 23: 1023–1028. doi:10.1016/0146-6380(95)00094-1.
Jump up ^ Muscoloa, A.; Bovalob, F.; Gionfriddob, F.; Nardi, S. (1999). "Earthworm humic matter produces auxin-like effects on Daucus carota cell growth and nitrate metabolism". Soil Biology and Biochemistry. 31: 1303–1311. doi:10.1016/S0038-0717(99)00049-8.
Jump up ^ Vermiculture
Jump up ^ Dungait, J. A.; Hopkins, D. W.; Gregory, A. S.; Whitmore, A. P. (2012). "Soil organic matter turnover is governed by accessibility not recalcitrance" (PDF). Global Change Biology. 18 (6): 1781–1796. doi:10.1111/j.1365-2486.2012.02665.x. Retrieved 30 August 2014. [permanent dead link]
Jump up ^ Oades, J. M. (1984). "Soil organic matter and structural stability: mechanisms and implications for management". Plant and soil. 76: 319–337. doi:10.1007/BF02205590. Retrieved 30 August 2014.
Jump up ^ Lehmann, J., Kern, D.C., Glaser, B., Woods, W.I., 2004. Amazonian Dark Earths: origin, properties, management. Springer, 523 pp. ISBN 978-1-4020-1839-8
Jump up ^ Hargitai, L (1993). "The soil of organic matter content and humus quality in the maintenance of soil fertility and in environmental protection". Landscape and Urban Planning. 27 (2–4): 161–167. doi:10.1016/0169-2046(93)90044-E.
Jump up ^ Hoitink, H.A.; Fahy, P.C. (1986). "Basic for the control of soilborne plant pathogens with composts". Annual Review of Phytopathology. 24: 93–114. doi:10.1146/annurev.py.24.090186.000521.
Jump up ^ C.Michael Hogan. 2010. Abiotic factor. Encyclopedia of Earth. eds Emily Monosson and C. Cleveland. National Council for Science and the Environment Archived 8 June 2013 at the Wayback Machine.. Washington DC
Jump up ^ De Macedo, J.R.; Do Amaral, Meneguelli; Ottoni, T.B.; Araujo, Jorge Araújo; de Sousa Lima, J. (2002). "Estimation of field capacity and moisture retention based on regression analysis involving chemical and physical properties in Alfisols and Ultisols of the state of Rio de Janeiro". Communications in Soil Science and Plant Analysis. 33 (13–14): 2037–2055. doi:10.1081/CSS-120005747.
Jump up ^ Hempfling, R.; Schulten, H.R.; Horn, R. (1990). "Relevance of humus composition to the physical/mechanical stability of agricultural soils: a study by direct pyrolysis-mass spectrometry". Journal of Analytical and Applied Pyrolysis. 17 (3): 275–281. doi:10.1016/0165-2370(90)85016-G.
Jump up ^ Soil Development: Soil Properties Archived 28 November 2012 at the Wayback Machine.
^ Jump up to: a b Szalay, A (1964). "Cation exchange properties of humic acids and their importance in the geochemical enrichment of UO2++ and other cations". Geochimica et Cosmochimica Acta. 28: 1605–1614. doi:10.1016/0016-7037(64)90009-2.
^ Jump up to: a b Elo, S.; Maunuksela, L.; Salkinoja-Salonen, M.; Smolander, A.; Haahtela, K. (2006). "Humus bacteria of Norway spruce stands: plant growth promoting properties and birch, red fescue and alder colonizing capacity". FEMS Microbiology Ecology. 31: 143–152. doi:10.1111/j.1574-6941.2000.tb00679.x.
^ Jump up to: a b Vreeken-Buijs, M.J.; Hassink, J.; Brussaard, L. (1998). "Relationships of soil microarthropod biomass with organic matter and pore size distribution in soils under different land use". Soil Biology and Biochemistry. 30: 97–106. doi:10.1016/S0038-0717(97)00064-3.
Jump up ^ Eyheraguibel, B.; Silvestrea, J. Morard (2008). "Effects of humic substances derived from organic waste enhancement on the growth and mineral nutrition of maize". Bioresource Technology. 99: 4206–4212. doi:10.1016/j.biortech.2007.08.082.
Jump up ^ Zandonadi, D. B.; Santos, M. P.; Busato, J. G.; Peres, L. E. P.; Façanha, A. R. (2013). "Plant physiology as affected by humified organic matter". Theoretical and Experimental Plant Physiology. 25: 13–25. doi:10.1590/S2197-00252013000100003. Retrieved 30 August 2014.
Jump up ^ Olness, A.; Archer, D. (2005). "Effect of organic carbon on available water in soil". Soil Science. 170: 90–101. doi:10.1097/00010694-200502000-00002.
Jump up ^ Effect of Organic Carbon on Available Water in Soil : Soil Science
Jump up ^ Kikuchi, R (2004). "Deacidification effect of the litter layer on forest soil during snowmelt runoff: laboratory experiment and its basic formularization for simulation modeling". Chemosphere. 54 (8): 1163–1169. doi:10.1016/j.chemosphere.2003.10.025. PMID 14664845.
Jump up ^ Caesar-Tonthat, T.C. (2002). "Soil binding properties of mucilage produced by a basidiomycete fungus in a model system". Mycological Research. 106 (8): 930–937. doi:10.1017/S0953756202006330.
Jump up ^ Huang, D.L.; Zeng, G.M.; Feng, C.L.; Hu, S.; Jiang, X.Y.; Tang, L.; Su, F.F.; Zhang, Y.; Zeng, W.; Liu, H.L. (2008). "Degradation of lead-contaminated lignocellulosic waste by Phanerochaete chrysosporium and the reduction of lead toxicity". Environmental Science and Technology. 42 (13): 4946–4951. Bibcode:2008EnST...42.4946H. doi:10.1021/es800072c. PMID 18678031.
External links[edit]
Find more aboutHumusat Wikipedia's sister projects
Definitions from Wiktionary
Quotations from Wikiquote
Jerzy Weber. "Types of humus in soils". Agricultural University of Wroclaw, Poland. Retrieved 2013-12-12.
Wershaw, R.L. "Evaluation of conceptual models of natural organic matter (humus) from a consideration of the chemical and biochemical processes of humification" (PDF). pubs.usgs.gov. USGS. Retrieved 14 March 2016.
IHSS. "What are Humic Substances?". International Humic Substances Society. Retrieved 19 February 2018.
Retrieved from "https://en.wikipedia.org/w/index.php?title=Humus&oldid=836895980"
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text:
What a Friend We Have in Jesus
From Wikipedia, the free encyclopedia
Jump to: navigation, search
"What a Friend We Have in Jesus"
Song
Genre
Hymn
Composer(s)
Charles C. Converse (1868)
Lyricist(s)
Joseph M. Scriven (1855)
"What a Friend We Have in Jesus" is a Christian hymn originally written by Joseph M. Scriven as a poem in 1855 to comfort his mother who was living in Ireland while he was in Canada. Scriven originally published the poem anonymously, and only received full credit for it in the 1880s.[1] The tune to the hymn was composed by Charles Crozat Converse in 1868. William Bolcom composed a setting of the hymn.
The hymn also has many versions with different lyrics in multiple languages. The Handbook to the Lutheran Hymnal notes, "In spite of the fact that this hymn, with its tune, has been criticized as being too much on the order of the sentimental gospel type, its popularity remains strong, and the hymn retains a place in modern hymnals."[2] In some settings, the lyrics have been matched to other tunes such as the Welsh "Calon Lân" (originally wedded to the Welsh poem translated as "A Pure Heart").
What a Friend We Have In Jesus
Performed by the Onward Brass Band
Problems playing this file? See media help.
Contents
[hide]
1 Renditions
1.1 In Asia
2 In popular culture
3 Published versions
4 References
5 External links
Renditions[edit]
Washington Phillips, as "Jesus Is My Friend" (1928, Columbia Records)[3][4]
Bing Crosby (1951, Beloved Hymns)
Rosemary Clooney (1959, Hymns from the Heart, MGM Records)
Ella Fitzgerald with the Ralph Carmichael Choir (1967, Brighten the Corner)
Aretha Franklin (1972, Amazing Grace)
Alan Price used the tune for his song "Changes" in the 1973 film O Lucky Man!, which was reused in a Volkswagen commercial of the same name with Paula Hamilton in the 1980s.[5]
Glen Campbell (1989, Favorite Hymns)
Driving Miss Daisy (1989) sung at Little Friendship Baptist Church in Atlanta, Georgia
Ike & Tina Turner (1974, The Gospel According to Ike & Tina)
The John Tesh Project (2000, Pure Hymns)[6]
Amy Grant recorded it as part of the medley "What a Friend We Have in Jesus/Old Rugged Cross/How Great Thou Art" on her 2002 studio album Legacy... Hymns and Faith, and later included on her 2015 compilation album Be Still and Know... Hymns & Faith.
Alan Jackson (2006, Precious Memories)
Brad Paisley (2008, Play)
Ronnie Milsap (2009, Then Sings My Soul)
Monty Alexander (2013, Uplift 2)[7]
In Asia[edit]
In Japan, the hymn's title was originally translated as "Itsukushimi Fukaki" (いつくしみ深き, lit. "Merciful"),[8] which is what it is best known by. In 1910, Daisui Sugitani re-wrote the lyrics in Japanese and changed the title to "Hoshi no Yo" (星の界, lit. "World of Stars"). Another version was written by Ryūkō Kawaji with the title "Hoshi no Sekai" (星の世界, lit. "World of Stars"). It is also known by the title "Tsumitoga o Ninou" (つみとがをにのう, lit. "To Bear Sin"). The hymn is popular at wedding ceremonies in Japan.[9]
In Indonesia, the hymn is known as "Yesus Kawan yang Sejati" and is sung in Indonesian or Batak (the indigenous language of North Sumatra) in Manado, Maluccan, and Protestant churches (around 6% of the population). Statistically, the majority of Indonesians are Muslim (around 76%) but native religion elements have up to 90% of the total population and consequently the hymn is widely known only among musicians, scholars and Indonesia's Christian community. However, prior to when Suharto seized power in 1967, the same music was adopted for a popular patriotic song titled "Ibu Pertiwi".
In Hindi, the hymn is a very important song and is sung as "Yeshu kaisa dost pyara". In Marathi, the hymn has been translated as "Kon Mitra Yeshuwani" By Mary Bessel.The song is common during solemn services (Passion week and burial). In Malayalam, the hymn as "Enthu Nallore sakhi Yesu" is sung to comfort and as an invitation to Christ.[10] This hymn had been translated into Telugu and it is sung during occasions as a song of comfort and solace. It is translated as "Preethi gala mana Yesu" and it is listed in the Andhra Kraisthava Keerthanalu (Andhra Christian hymnals) as hymn No. 407.
In India, the hymn sung in Konkani, "Dulob Jezu", was translated by Felix Paul Noronha of Mangalore.
In popular culture[edit]
This section indiscriminately collects miscellaneous information. Please compress this material to remove any irrelevant or unimportant information. (February 2018)
A version was sung during World War I with the line "When this bloody war is over" in place of the original title.[9] The tune was used in the 1969 film, Oh! What a Lovely War with the title "When This Lousy War Is Over". The tune was used in Alan Price's song Changes, which was written for the 1973 film O Lucky Man! and later became a hit when used in the 1987 Volkswagen Golf television commercial. The tune was in the labor protest movement due to its wide popularity. "Dump the Bosses Off Your Backs" (words by John Brill) was published in the IWW "Little Red Songbook" and has been recorded by dozens of artists including Utah Phillips, Anne Feeney, and Joe Glazer. A Norwegian version was used in the film Trollhunter.
Published versions[edit]
Rise Up Singing, page 98
The Lutheran Hymnal, hymn #457
References[edit]
Wikisource has original text related to this article:
What a Friend We Have in Jesus
Jump up ^ "What a Friend We Have in Jesus". Retrieved 2007-05-03.
Jump up ^ Polack, W.G. (1941). Handbook to the Lutheran Hymnal. St. Louis: Concordia. p. 323.
Jump up ^ "Washington Phillips discography". wirz.de. Retrieved August 24, 2015.
Jump up ^ George Washington Phillips: Jesus Is My Friend at AllMusic. Retrieved August 24, 2015.
Jump up ^ "Volkswagen Golf – Paula Hamilton – 1987 – UK Advert". Retro Commercials. March 13, 2010. Retrieved September 26, 2011.
Jump up ^ "Pure Hymns overview". Allmusic. Retrieved July 4, 2010.
Jump up ^ "Monty Alexander UPLIFT 2". Jazz Legacy Productions. Retrieved January 11, 2014.
Jump up ^ "Itsukushimi Fukaki song sheet" (PDF). Retrieved 2007-07-16.
^ Jump up to: a b "312: What a Friend We Have in Jesus". Retrieved 2008-03-19.
Jump up ^ Christhiya Keerthanangal (Christian Hymns). 2007. Hymn 173.
External links[edit]
Piano score (pdf) at Timeless Truths
Text, MIDI, and piano score for "What a Friend We Have in Jesus" at HymnSite.com
"What a Friend We Have in Jesus" Mp3 and lyrics
[hide]
v
t
e
Washington Phillips
Original Columbia
78 rpm records
(chronological)
"Lift Him Up That's All" / "Take Your Burden to the Lord and Leave It There"
"Denomination Blues – Part 1" / "Denomination Blues – Part 2"
"Mother's Last Word to Her Son" / "Paul and Silas in Jail"
"What Are They Doing in Heaven Today" / "Jesus Is My Friend"
"I Am Born to Preach the Gospel" / "Train Your Child"
"A Mother's Last Word to Her Daughter" / "I've Got the Key to the Kingdom"
"I Had a Good Father and Mother" / "The Church Needs Good Deacons"
Later song
releases
"You Can't Stop a Tattler – Part 1" "You Can't Stop a Tattler – Part 2"
Related articles
List of songs (with recording & catalogue details)
Retrieved from "https://en.wikipedia.org/w/index.php?title=What_a_Friend_We_Have_in_Jesus&oldid=831327264"
Categories:
1928 songs
Canadian Christian hymns
Columbia Records singles
Glen Campbell songs
Mississippi John Hurt songs
Pace Jubilee Singers songs
Songs about Jesus
Washington Phillips songs
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Wikipedia:Media help

values: Then Sings My Soul (Ronnie Milsap album)

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Hindi language

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Passion week

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Wikipedia:Trivia sections

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values: wikisource:Special:Search/What a Friend We Have in Jesus

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http://www.wirz.de/music/philwfrm.htm

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https://www.allmusic.com/album/r500795

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78 rpm record

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values: List of songs recorded by Washington Phillips

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values: いつくしみ深き – Japanese

values: What a Friend We Have in Jesus – Norwegian

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