The DOI matches its Crossref record; 696 of the 701 references it cites were found in a registry or an index.
Energy conservation in chemotrophic anaerobic bacteria
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“Such findings are broadly consistent with the findings of Thauer et al. [39] that under conditions relevant for microbes, in the reaction of H2 with CO2, the equilibrium lies on the side of reduced carbon compounds, which is why acetogens can grow from the reaction2.3with ΔG°′ = –104.6 kJ mol−1 [39] and methanogens can grow from the reaction2.4with ΔG°′ = –131 kJ mol−1 [40] as their sole source of”
From Early bioenergetic evolution (2013) · cites this paper as [39]
In the citing paper
“For Moorella, HdrABC homologues are encoded directly next to the gene for methylene-H4F reductase, which catalyses a very exergonic reaction and was therefore once suggested as a coupling site for energy conservation [39].”
From Early bioenergetic evolution (2013) · cites this paper as [39]
In the citing paper
“Additionally, ethanol production from CO is thermodynamically favorable over CO2 (Reactions 1-4; the free energy (ΔG°') of Reactions 1–4 was calculated from data given in Thauer et al. (1977)).”
From Gas Fermentation—A Flexible Platform for Commercial Scale Production of Low-Carbon-Fuels and Chemicals from Waste and Renewable Feedstocks (2016) · cites this paper as Thauer et al., 1977
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The Reduction of Sulphur Compounds by Desulphovibrio desulphuricans
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FERMENTATION OF ETHYLENE GLYCOL BYCLOSTRIDIUM GLYCOLICUM, SP. N
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STUDIES ON THERMOPHILIC SULFATE-REDUCING BACTERIA III
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Coenzyme A-linked Aldehyde Dehydrogenase from Escherichia coli
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Proton translocation induced by ATPase activity in chloroplasts
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Branched Electron-Transport Systems in Bacteria
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Sucrose Catabolism in Clostridium pasteurianum and Its Relation to N 2 Fixation
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Regulation of reductase formation in Proteus mirabilis
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Biochemistry of the Sulfur Cycle
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Total synthesis of acetate from CO2
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Production of Nitric Oxide and Nitrous Oxide During Denitrification by Corynebacterium nephridii
Renner, E. D., & Becker, G. E. (1970) · Journal of Bacteriology · doi:10.1128/jb.101.3.821-826.1970 · Cited by 82
Enzymatic Studies of Pure Cultures of Rumen Microorganisms
Joyner, A. E., & Baldwin, R. L. (1966) · Journal of Bacteriology · doi:10.1128/jb.92.5.1321-1330.1966 · Cited by 82
Purification and Properties of Electron-transferring Flavoprotein from Peptostreptococcus elsdenii
Whitfield, C. D., & Mayhew, S. G. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42700-2 · Cited by 82
On the Role of Quinones in Bacterial Electron Transport
Kröger, A., Dadák, V., Klingenberg, M., & Diemer, F. (1971) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1971.tb01472.x · Cited by 81
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H2-dependent anaerobic growth of Escherichia coli on L-malate: succinate formation
Macy, J. M., Kulla, H. G., & Gottschalk, G. (1976) · Journal of Bacteriology · doi:10.1128/jb.125.2.423-428.1976 · Cited by 80
Conversion of Light to Chemical Free Energy
Eisenstein, K. K., & Wang, J. H. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91743-6 · Cited by 80
CARBOHYDRATE METABOLISM IN MICROORGANISMS
Anderson, R. L., & Wood, W. A. (1969) · Annual Review of Microbiology · doi:10.1146/annurev.mi.23.100169.002543 · Cited by 80
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Thauer, R. K. (1972) · FEBS Letters · doi:10.1016/0014-5793(72)80421-6 · Cited by 79
Self-citationMembrane Adenosine Triphosphatase from Streptococcus faecalis
Schnebli, H. P., & Abrams, A. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63296-x · Cited by 79
The Mechanism of Ion Translocation in Mitochondria. 3. Coupling of K+ Efflux with ATP Synthesis
Rossi, E. M. C., & AZZONE, G. F. (1970) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1970.tb00853.x · Cited by 79
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The evolution of chemiosmotic energy coupling
Raven, J. A., & SMITH, F. A. (1976) · Journal of Theoretical Biology · doi:10.1016/0022-5193(76)90003-5 · Cited by 78
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The proton‐translocating ATPase of Escherichia coli
West, I. C., & Mitchell, P. D. (1974) · FEBS Letters · doi:10.1016/0014-5793(74)80880-x · Cited by 77
A Nitrite Reductase from Achromobacter cycloclastes
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Characteristics of S Organism Isolated from Methanobacillus omelianskii
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REDUCTION OF FERRIC HYDROXIDE BY STRAINS OF BACILLUS POLYMYXA
ROBERTS, J. L. (1947) · Soil Science · doi:10.1097/00010694-194702000-00006 · Cited by 76
Chemical study of two flavodoxins extracted from sulfate reducing bacteria
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The Physiology of Sulphate-Reducing Bacteria
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Purification and properties of a c-type cytochrome from Micrococcus denitrificans
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Fermentation of Fructose and Synthesis of Acetate from Carbon Dioxide by Clostridium formicoaceticum
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Hamster Brown‐Adipose‐Tissue Mitochondria
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Purification and properties of acetate kinase from Clostridium thermoaceticum
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Lactic Acid Translocation: Terminal Step in Glycolysis by Streptococcus faecalis
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Cytochrome c-557 (551) and Cytochrome cd of Alcaligenes faecalis
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The Pyruvate-Phosphate Dikinase Reaction
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Considerations on the energy metabolism of Clostridium kluyveri
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The two faces of the inner mitochondrial membrane.
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Siroheme: a prosthetic group of the Neurospora crassa assimilatory nitrite reductase.
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Nitrate reductase system in Staphylococcus aureus wild type and mutants
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Mechanism of Propionate Formation by Selenomonas ruminantium, a Rumen Micro-organism
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Are thiosulfate and trithionate intermediates in dissimilatory sulfate reduction?
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Estimations of membrane potentials in Streptococcus faecalis by means of a fluorescent probe
Laris, P. C., & Pershadsingh, H. A. (1974) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(74)90591-9 · Cited by 65
Aerobic and anaerobic respiration in Micrococcus denitrificans
Lam, Y., & Nicholas, D. J. D. (1969) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(69)90141-8 · Cited by 65
Solubilization of Escherichia coli nitrate reductase by a membrane-bound protease
MacGregor, C. H. (1975) · Journal of Bacteriology · doi:10.1128/jb.121.3.1102-1110.1975 · Cited by 65
The Mechanism of Propionic Acid Formation by Clostridium propionicum
Johns, A. T. (1952) · Journal of General Microbiology · doi:10.1099/00221287-6-1-2-123 · Cited by 65
Cytochrome c-551.5 (c7) from Desulfuromonas acetoxidans
Probst, I., Bruschi, M., Pfennig, N., & LeGall, J. (1977) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(77)90151-7 · Cited by 65
Biochemical Studies on Sulfate-reducing Bacteria
Kobayashi, K., Seki, Y., & Ishimoto, M. (1974) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a130420 · Cited by 64
Electron Transfer and Energy Conservation
Williams, R. J. P. (1969) · Current topics in bioenergetics · doi:10.1016/b978-1-4831-9971-9.50009-2 · Cited by 64
Total Synthesis of Acetate from CO2
Schulman, M., Ghambeer, R. K., Ljungdahl, L. G., & Wood, H. G. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43441-8 · Cited by 64
Klein, S. M., & Sagers, R. D. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81463-1 · Cited by 64
Advertisement: Clark's Oxidation Reduction Potentials of Organic Systems
Clark, W. (1960) · The Journal of Physical Chemistry · doi:10.1021/j100830a600 · Cited by 64
Lm, S., & WIMPENNY, J. W. T. (1972) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(72)90126-0 · Cited by 64
Lester, R. L., White, D. C., & Smith, S. L. (1964) · Biochemistry · doi:10.1021/bi00895a018 · Cited by 64
Li, L.-F., Ljungdahl, L. G., & Wood, H. G. (1966) · Journal of Bacteriology · doi:10.1128/jb.92.2.405-412.1966 · Cited by 63
Comparative ultrastructure of methanogenic bacteria
Zeikus, J. G., & Bowen, V. G. (1975) · Canadian Journal of Microbiology · doi:10.1139/m75-019 · Cited by 63
Proton‐driven phosphorylation reactions in mitochondrial and chloroplast membranes
Williams, R. J. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80001-9 · Cited by 62
The occurrence of a modified Entner-Doudoroff pathway in Clostridium aceticum
Andreesen, J. R., & Gottschalk, G. (1969) · Archives of Microbiology · doi:10.1007/bf00409760 · Cited by 62
STUDIES ON THE ENZYMIC REDUCTION OF AMINO ACIDS
Stadtman, T. C., Elliott, P., & Tiemann, L. (1958) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70459-6 · Cited by 62
Some properties of a nitrate reductase from Pseudomonas denitrificans
Radcliffe, B. C., & Nicholas, D. J. D. (1970) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(70)90257-4 · Cited by 62
Pentose phosphate cleavage by Leuconostoc mesenteroides
Hurwitz, J. (1958) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(58)90526-2 · Cited by 62
The biosynthesis of alanine by Clostridium kluyveri
Andrew, I., & Morris, J. G. (1965) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(65)90292-8 · Cited by 62
Properties of two clostridial flavodoxins
Mayhew, S. G. (1971) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(71)90206-3 · Cited by 62
Purification and some properties of nitrate reductase (EC 1.7.99.4) from Escherichia coli K12
CLEGG, R. A. (1976) · Biochemical Journal · doi:10.1042/bj1530533 · Cited by 61
LEACH, C. K., & Carr, N. G. (1971) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(71)90019-3 · Cited by 61
Formate: Cytochrome Oxidoreductase of Desulfovibrio vulgaris
Yagi, T. (1969) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a129171 · Cited by 61
Specificity of the Heme Requirement for Growth of Bacteroides ruminicola
Caldwell, D. R., White, D. C., Bryant, M. P., & Doetsch, R. N. (1965) · Journal of Bacteriology · doi:10.1128/jb.90.6.1645-1654.1965 · Cited by 60
Role of Carbon Dioxide and Acetate in Biosynthesis by Sulphate-reducing Bacteria
Sorokin, Y. I. (1966) · Nature · doi:10.1038/210551a0 · Cited by 60
Uncoupling in Bacterial Growth: Effect of Pantothenate Starvation on Growth of Zymomonas mobilis
Belaïch, J. P., Belaich, A., & Simonpietri, P. (1972) · Journal of General Microbiology · doi:10.1099/00221287-70-2-179 · Cited by 60
ENZYMIC GENERATORS OF MEMBRANE POTENTIAL IN MITOCHONDRIA
Skulachev, V. P. (1974) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1974.tb14384.x · Cited by 60
Hardman, J. K., & Stadtman, T. C. (1960) · Journal of Bacteriology · doi:10.1128/jb.79.4.544-548.1960 · Cited by 60
Thauer, R. K., Rupprecht, E., Ohrloff, C., Jungermann, K. A., & Decker, K. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62416-0 · Cited by 60
Self-citationIdentity of Pseudomonas Cytochrome Oxidase with Pseudomonas Nitrite Redcutase
YAMANAKA, T. (1964) · Nature · doi:10.1038/204253a0 · Cited by 59
Energetics and Kinetics of Anaerobic Treatment
McCarty, P. L. (1971) · Advances in chemistry series · doi:10.1021/ba-1971-0105.ch006 · Cited by 59
The fermentation of lactate and acrylate by the rumen micro-organism lc
Ladd, J. N., & Walker, D. J. (1959) · Biochemical Journal · doi:10.1042/bj0710364 · Cited by 59
The free energy change associated with the hydrolysis of the thiol ester bond of acetyl coenzyme A
Burton, K. (1955) · Biochemical Journal · doi:10.1042/bj0590044 · Cited by 59
Barton, L. L., LeGall, J., & Peck, H. D. (1970) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(70)90189-0 · Cited by 58
Electron Carriers for the Phosphoroclastic Reaction of Desulfovibrio desulfuricans
Akagi, J. M. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)95987-9 · Cited by 58
Haas, D. W. (1964) · Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects · doi:10.1016/0926-6569(64)90002-1 · Cited by 58
Separation of soluble denitrifying enzymes and cytochromes from Pseudomonas perfectomarinus
Cox, C. D., Jr., & Payne, W. J. (1973) · Canadian Journal of Microbiology · doi:10.1139/m73-137 · Cited by 58
Bothe, H., Falkenberg, B., & Nolteernsting, U. (1974) · Archives of Microbiology · doi:10.1007/bf00590185 · Cited by 57
Methylmalonyl Coenzyme A Decarboxylase
Galivan, J. H., & Allen, S. H. G. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)56980-0 · Cited by 57
Cobamide-dependent methanol-cyanocob(I)alamin methyltransferase of Methanosarcina barkeri
Blaylock, B. A. (1968) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(68)90333-0 · Cited by 57
Growth of Sulphate-reducing Bacteria by Fumarate Dismutation
Miller, J. D., & Wakerley, D. S. (1966) · Journal of General Microbiology · doi:10.1099/00221287-43-1-101 · Cited by 57
Shum, A. C., & Murphy, J. C. (1972) · Journal of Bacteriology · doi:10.1128/jb.110.1.447-449.1972 · Cited by 56
Ambler, R. P. (1971) · FEBS Letters · doi:10.1016/0014-5793(71)80484-2 · Cited by 56
Cytochrome c552 and nitrite reduction in Escherichia coli
Cole, J. A. (1968) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(68)90122-9 · Cited by 56
Ottow, J. C. G. (1970) · Journal of Basic Microbiology · doi:10.1002/jobm.3630100105 · Cited by 56
Stadtman, T. C. (1966) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(66)90151-2 · Cited by 56
Energy transduction and proton translocation by adenosine triphosphatases
Boyer, P. D. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80464-9 · Cited by 55
Purification, characterization and properties of nitrite reductase of Achromobacter fischeri
Prakash, O., & Sadana, J. C. (1972) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(72)90181-6 · Cited by 55
Biosynthesis of methane from the methyl moiety of methylcobalamin
Blaylock, B. A., & Stadtman, T. C. (1963) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(63)90023-8 · Cited by 55
de Vries, W., van Wijck-Kapteyn, W. M. C., & Oosterhuis, S. K. H. (2000) · Microbiology · doi:10.1099/00221287-81-1-69 · Cited by 55
Proton translocation quotient for the adenosine triphosphatase of rat liver mitochondria
Moyle, J., & Mitchell, P. D. (1973) · FEBS Letters · doi:10.1016/0014-5793(73)80678-7 · Cited by 55
Griniuvienė, B., Chmieliauskaitė, V., & Grinius, L. (1974) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(74)80335-9 · Cited by 54
Thauer, R. K., Käufer, B., & Fuchs, G. (1975) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1975.tb02143.x · Cited by 54
Self-citationSTUDIES ON SUCCINIC DEHYDROGENASE
Warringa, M. G. P. J., Smith, O. H., Giuditta, A., & Singer, T. P. (1958) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70544-9 · Cited by 54
Meyer, T. E., Bartsch, R. G., & Kamen, M. D. (1971) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(71)90162-9 · Cited by 54
ATP Pool and Growth Yield in Selenomonas ruminantium
Hobson, P. N., & SUMMERS, R. (1972) · Journal of General Microbiology · doi:10.1099/00221287-70-2-351 · Cited by 54
Sulfate Activation and Transfer
Humberto, R., & Meio, D. (1975) · Elsevier eBooks · doi:10.1016/b978-0-12-299257-5.50015-4 · Cited by 53
Stereochemistry of the Glutamate Mutase Reaction
Sprecher, M., Switzer, R. L., & Sprinson, D. B. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96844-4 · Cited by 53
Membrane potential as a driving force for ATP synthesis in chloroplasts
Schuldiner, S., Rottenberg, H., & Avron, M. (1972) · FEBS Letters · doi:10.1016/0014-5793(72)80704-x · Cited by 53
Propylation and Purification of a B12 Enzyme Involved in Methane Formation*
Wood, J., & WOLFE, R. S. (1966) · Biochemistry · doi:10.1021/bi00875a031 · Cited by 53
Anaerobic transport in Escherichia coli membrane vesicles.
Boonstra, J., Huttunen, M. T., & Konings, W. N. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41001-6 · Cited by 53
Nitrite Reductase-deficient Mutants of Escherichia coli K12
Cole, J. A., & Ward, F. B. (1973) · Journal of General Microbiology · doi:10.1099/00221287-76-1-21 · Cited by 52
Cytochromes in Streptococcus faecalis var. zymogenes Grown in a Haematin-containing Medium
RITCHEY, T. W., & Seeley, H. W. (1974) · Journal of General Microbiology · doi:10.1099/00221287-85-2-220 · Cited by 52
Energy Coupling of the β-Methylgalactoside Transport System of Escherichia coli
Parnes, J. R., & Boos, W. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43787-3 · Cited by 52
National Bureau of Standards, W., Wagman, D. D., Evans, W., Parker, V. B., Halow, I., Bailey, S., Schumm, R. H., & Churney, K. L. (1971) · doi:10.2172/4021549 · Cited by 52
Bray, R. C., Vincent, S. P., Lowe, D. J., CLEGG, R. A., & Garland, P. B. (1976) · Biochemical Journal · doi:10.1042/bj1550201 · Cited by 52
Pathway of propionate formation in Bacteroides ruminicola
Wallnöfer, P. R., & Baldwin, R. L. (1967) · Journal of Bacteriology · doi:10.1128/jb.93.1.504-505.1967 · Cited by 51
Brockman, H. L., & Wood, W. A. (1975) · Journal of Bacteriology · doi:10.1128/jb.124.3.1447-1453.1975 · Cited by 51
Holländer, R. (1976) · FEBS Letters · doi:10.1016/0014-5793(76)80821-6 · Cited by 51
Green butyryl-coenzyme A dehydrogenase. An enzyme–acyl-coenzyme A complex
Engel, P. C., & Massey, V. (1971) · Biochemical Journal · doi:10.1042/bj1250889 · Cited by 51
Purification and Characterization of Component S of Glutamate Mutase
Switzer, R. L., & Barker, H. A. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99621-3 · Cited by 51
Electron Transport System of the Protoheme-requiring Anaerobe Bacteroides melaninogenicus
Rizza, V., Sinclair, P. R., White, D. C., & Cuorant, P. R. (1968) · Journal of Bacteriology · doi:10.1128/jb.96.3.665-671.1968 · Cited by 51
Ottow, J. C. G. (1968) · Zeitschrift für allgemeine Mikrobiologie · doi:10.1002/jobm.19680080512 · Cited by 51
The Mechanism of Propionic Acid Formation by Propionibacteria
Johns, A. T. (1951) · Journal of General Microbiology · doi:10.1099/00221287-5-2-337 · Cited by 51
Flagged first, then by citations
5 of the 701 references couldn’t be matched to a known paper.
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Microbial Fuel Cells: Methodology and Technology
Logan, B. E., Hamelers, H. V. M., Rozendal, R. A., Schröder, U., Keller, J., Freguia, S., Aelterman, P., Verstraete, W., & Rabaey, K. (2006) · Environmental Science & Technology · doi:10.1021/es0605016 · Cited by 6,095
Host-Bacterial Mutualism in the Human Intestine
Bäckhed, F., Ley, R. E., Sonnenburg, J. L., Peterson, D. A., & Gordon, J. I. (2005) · Science · doi:10.1126/science.1104816 · Cited by 5,277
Ecological and Evolutionary Forces Shaping Microbial Diversity in the Human Intestine
Ley, R. E., Peterson, D. A., & Gordon, J. I. (2006) · Cell · doi:10.1016/j.cell.2006.02.017 · Cited by 3,358
Methanogens: reevaluation of a unique biological group
Balch, W. E., Fox, G. E., Magrum, L. J., Woese, C. R., & WOLFE, R. S. (1979) · Microbiological Reviews · doi:10.1128/mr.43.2.260-296.1979 · Cited by 2,918
The ecology and biotechnology of sulphate-reducing bacteria
Muyzer, G., & Stams, A. J. M. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro1892 · Cited by 2,528
Metadata
- Authors
- Thauer, R. K., Jungermann, K., & Decker, K.
- ORCID
- Thauer, R K
- Venue
- Bacteriological Reviews
- Publisher
- American Society for Microbiology
- Published
- 1977-03
- Volume
- 41
- Issue
- 1
- Pages
- 100-180
- ISSN
- 0005-3678 (ISSN-L)
- PMC
- PMC413997
- OpenAlex
- W2112951169
- Cited by
- 4,146
- References
- 701
- Citations by year
- 2026: 108 · 2025: 91 · 2024: 88 · 2023: 112 · 2022: 114 · 2021: 126 · 2020: 121 · 2019: 145 · 2018: 152 · 2017: 140 · 2016: 135 · 2015: 120 · 2014: 144 · 2013: 133 · 2012: 114
- FWCI
- 311.40
- Type
- journal article
- Language
- en
- Update notices
- correction (1977-09-01)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Bacteriological Reviews (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Bayerische Staatsbibliothek (submittedVersion)
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Anaerobic Digestion and Biogas Production
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- energy conservation, chemotrophic bacteria, anaerobic bacteria, anaerobic metabolism, energy metabolism
- MeSH terms
- Adenosine Triphosphate, Anaerobiosis, Bacteria, Cell Membrane, Energy Metabolism, Fermentation, Glucose, Hydrogenation
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