Cited by 4,146Anaerobic Digestion and Biogas ProductionMicrobial metabolism and enzyme functionBacterial Genetics and Biotechnology

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Energy conservation in chemotrophic anaerobic bacteria

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Thauer, R K, Jungermann, K, Decker, K·1977·Bacteriological Reviews

DOI 10.1128/br.41.1.100-180.1977PMC PMC413997

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Items 401–600 of 696

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Intermediary Metabolism of the Liver FlukeFasciola hepatica,I. Biosynthesis of Propionic acid
ZOETEN, L. W. D., POSTHUMA, D., & Tipker, J. (1969) · Hoppe-Seyler´s Zeitschrift für physiologische Chemie · doi:10.1515/bchm2.1969.350.1.683 · Cited by 49
SYNTHESIS OF ACETATE FROM FORMATE AND CARBON DIOXIDE BY CLOSTRIDIUM THERMOACETICUM
Lentz, K. E., & Wood, H. G. (1955) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65987-3 · Cited by 48
4 Multienzyme Complexes
Reed, L. J., & Cox, D. J. (1970) · The Enzymes · doi:10.1016/s1874-6047(08)60167-5 · Cited by 48
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Evidence for the presence of a b-type cytochrome in the sulfate-reducing bacterium Desulfovibrio gigas, and its role in the reduction of fumarate by molecular hydrogen
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The lactic dehydrogenase of Propionibacterium pentosaceum
Molinari, R., & Lara, F. J. S. (1960) · Biochemical Journal · doi:10.1042/bj0750057 · Cited by 48
Total Synthesis of Acetate from CO 2 : Methyltetrahydrofolate, an Intermediate, and a Procedure for Separation of the Folates
Parker, D. J., Wu, T.-F. L., & Wood, H. G. (1971) · Journal of Bacteriology · doi:10.1128/jb.108.2.770-776.1971 · Cited by 47
[124a] Carbamyl phosphate synthesis and utilization
Jones, M. E. (1962) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(62)05336-7 · Cited by 47
Effect of Nitrate, Fumarate, and Oxygen on the Formation of the Membrane-Bound Electron Transport System of Haemophilus parainfluenzae
Sinclair, P. R., & White, D. C. (1970) · Journal of Bacteriology · doi:10.1128/jb.101.2.365-372.1970 · Cited by 47
Biochemical Cytology of Trichomonad Flagellates. II. Subcellular Distribution of Oxidoreductases and Hydrolases in Monocercomonas sp.*
Lindmark, D. G., & Müller, M. (1974) · The Journal of Protozoology · doi:10.1111/j.1550-7408.1974.tb03673.x · Cited by 47
Purification and Role of Phosphotransbutyrylase
Valentine, R. C., & WOLFE, R. S. (1960) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69341-x · Cited by 47
Isolation of 2-Solanesyl-1,4-naphthoquinone from Streptococcus faecalis, 10 Cl
Baum, R. H., & Dolin, M. I. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97235-2 · Cited by 46
The fermentation of l -threonine, l -serine, l -cysteine and acrylic acid by a Gram-negative coccus
Lewis, D., & Elsden, S. R. (1955) · Biochemical Journal · doi:10.1042/bj0600683 · Cited by 46
Phosphorylation associated with nitrate and nitrite reduction in Micrococcus denitrificans and Pseudomonas denitrificans
Naik, M. S., & Nicholas, D. J. D. (1966) · Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation · doi:10.1016/s0926-6593(66)80007-3 · Cited by 46
Comparative biochemistry of the biological reduction of fumaric acid
Peck, H. D., Smith, O. H., & Gest, H. (1957) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(57)90431-6 · Cited by 46
An iron tetrahydroporphyrin prosthetic group common to both assimilatory and dissimilatory sulfite reductases
Murphy, M. J., Siegel, L. M., Kamin, H., DerVartanian, D. V., Lee, J.-P., LeGall, J., & Peck, H. D. (1973) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(73)90891-7 · Cited by 46
Ferredoxin- and Nicotinamide Adenine Dinucleotide-Dependent H 2 Production from Ethanol and Formate in Extracts of S Organism Isolated from “Methanobacillus omelianskii”
Reddy, C. A., Bryant, M. P., & Wolin, M. J. (1972) · Journal of Bacteriology · doi:10.1128/jb.110.1.126-132.1972 · Cited by 45
Hydrogen formation from NADH in cell‐free extracts of Clostridium kluyveri
Thauer, R. K., Jungermann, K. A., Rupprecht, E., & Decker, K. (1969) · FEBS Letters · doi:10.1016/0014-5793(69)80208-5 · Cited by 45
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12. Bacterial Membrane ATPase
Abrams, A., & Smith, J. B. (1974) · The Enzymes · doi:10.1016/s1874-6047(08)60144-4 · Cited by 45
Anaerobic degradation of lysine
Stadtman, T. C., & Renz, P. (1968) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(68)90657-7 · Cited by 45
ROLE OF BUTYRYL PHOSPHATE IN THE ENERGY METABOLISM OF CLOSTRIDIUM TETANOMORPHUM
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A soluble c-type cytochrome from anaerobically grown Escherichia coli and various Enterobacteriaceae
Gray, C. T., WIMPENNY, J. W. T., Hughes, D. E., & Ranlett, M. (1963) · Biochimica et Biophysica Acta · doi:10.1016/0926-6569(63)90220-7 · Cited by 45
Studies on Soluble Cytochromes in Enterobacteriaceae
Fujita, T., & Sato, R. (1966) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a128495 · Cited by 44
Glucose and fructose metabolism in Zymomonas anaerobia
McGill, D., & DAWES, E. A. (1971) · Biochemical Journal · doi:10.1042/bj1251059 · Cited by 44
Anaerobic Electron Transfer and Active Transport in Bacteria
Konings, W. N., & Boonstra, J. (1977) · Current topics in membranes and transport · doi:10.1016/s0070-2161(08)60679-6 · Cited by 44
The Purification and Properties of the Hydrogenase of Desulfovibrio desulfuricans
Krasna, A. I., RIKLIS, E., & Rittenberg, D. (1960) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)76942-7 · Cited by 44
Anaerobic Growth Yields of Aerobacter cloacae and Escherichia coli
Hernandez, E., & Johnson, M. J. (1967) · Journal of Bacteriology · doi:10.1128/jb.94.4.991-995.1967 · Cited by 44
Transient pH changes during D-lactate oxidation by membrane vesicles
Reeves, J. P. (1971) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(71)90427-x · Cited by 44
ATP requirement for methanogenesis in cell extracts of methanobacterium strain M.o.H.
Roberton, A. M., & WOLFE, R. S. (1969) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(69)90391-2 · Cited by 44
Redox Potentials of Certain Vitamins K: Implications for a Role in Sulfite Reduction by Obligately Anaerobic Bacteria
Wagner, G. C., Kassner, R. J., & Kamen, M. D. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.2.253 · Cited by 44
Solubilization and Properties of Formate Dehydrogenase and Cytochrome b1 from Escherichia coli*
Itagaki, E., Fujita, T., & Sato, R. (1962) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a127581 · Cited by 44
Studies on Denitrification
Matsubara, T. (1971) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a129572 · Cited by 44
Path of Glucose Breakdown and Cell Yields of a Facultative Anaerobe, Actinomyces naeslundii
Buchanan, B. B., & Pine, L. (1967) · Journal of General Microbiology · doi:10.1099/00221287-46-2-225 · Cited by 43
Enzymatic Phosphorylation of Butyrate
Twarog, R., & WOLFE, R. S. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)73776-4 · Cited by 43
Influence of Nitrate on Fermentation Pattern, Molar Growth Yields and Synthesis of Cytochrome b in Propionibacterium pentosaceum
van Gent-Ruijters, M. L. W., de Vries, W., & Stouthamer, A. H. (1975) · Journal of General Microbiology · doi:10.1099/00221287-88-1-36 · Cited by 43
Formyltetrahydrofolate Synthetase
Himes, R. H., & Rabinowitz, J. C. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60250-9 · Cited by 42
Proton Translocation in Chloroplasts1 1Abbreviations used in this article: DPIP and DPIPH2, oxidized and reduced form of 2,6-dichlorophenolindophenol; DAD, 2,3,5,6-tetramethyl-p-phenylenediamine (diaminodurene); TMPD, N,N,N′,N′-tetramethyl-p-phenylenediamine; DMPD, N,N-dimethyl-p-phenylenediamine; PMS, N-methyl-phenazonium methosulfate; MV, methyl viologen (N,N′-dimethyl-4,4′-dipyridylium dichloride); AQ, anthraquinone-2-sulfonate; FCCP, carbonylcyanide-p-trifluoromethoxy-phenylhydrazone; DNP, 2,4-dinitrophenol; DCCD, dicyclohexyl-carbodiimide; EDAC, l-ethyl-3-(3-dimethylaminopropyl)-carbodiimide; CF1, coupling factor 1 of chloroplasts (site of ATP synthesis); CF0, a membrane component to which CF1 is attached. For further abbreviations, see legends.
Hauska, G. A., & Trebst, A. (1977) · Current topics in bioenergetics · doi:10.1016/b978-0-12-152506-4.50011-x · Cited by 42
Studies on Denitrification
Miyata, M., & Mori, T. (1969) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a129170 · Cited by 42
11. Mitochondrial and Chloroplast ATPases
Penefsky, H. S. (1974) · The Enzymes · doi:10.1016/s1874-6047(08)60143-2 · Cited by 42
DEGRADATION OF PYRUVATE BY MICROCOCCUS LACTILYTICUS I
McCormick, N. G., Ordal, E. J., & Whiteley, H. R. (1962) · Journal of Bacteriology · doi:10.1128/jb.83.4.887-898.1962 · Cited by 42
Denitrification by Corynebacterium nephridii
Hart, L. T., Larson, A. D., & McCleskey, C. S. (1965) · Journal of Bacteriology · doi:10.1128/jb.89.4.1104-1108.1965 · Cited by 42
The Methane Fermentations
Pine, M. J. (1971) · Advances in chemistry series · doi:10.1021/ba-1971-0105.ch001 · Cited by 42
Fermentation of Agmatine in Streptococcus faecalis: Occurrence of Putrescine Transcarbamoylase
Roon, R. J., & Barker, H. A. (1972) · Journal of Bacteriology · doi:10.1128/jb.109.1.44-50.1972 · Cited by 41
The synthesis of one‐carbon units from CO2 via a new ferredoxin dependent monocarboxylic acid cycle
Thauer, R. K., Rupprecht, E., & Jungermann, K. A. (1970) · FEBS Letters · doi:10.1016/0014-5793(70)80293-9 · Cited by 41
Self-citation
Membrane permeability and internal volume as factors in ATP synthesis by spinach chloroplasts
Uribe, E. G., & Jagendorf, A. T. (1968) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(68)90041-6 · Cited by 41
Carbamyl and Acetyl Phosphokinase Activities of Streptococcus faecalis and Escherichia coli
Thorne, K. J. I., & Jones, M. E. (1963) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)51856-1 · Cited by 41
Glycine Metabolism
Klein, S. M., & Sagers, R. D. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81464-3 · Cited by 41
Behavior of purified arginine desiminase from S. faecalis
Petrack, B., Sullivan, L., & Ratner, S. (1957) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(57)90485-x · Cited by 41
Ferredoxin mediated hydrogen formation from NADPH in a cell‐free system of Clostridium kluyveri
Jungermann, K. A., Thauer, R. K., Rupprecht, E., Ohrloff, C., & Decker, K. (1969) · FEBS Letters · doi:10.1016/0014-5793(69)80119-5 · Cited by 41
Self-citation
Molar Growth Yields of Certain Lactic Acid Bacteria as Influenced by Autolysis
Moustafa, H. H., & Collins, E. B. (1968) · Journal of Bacteriology · doi:10.1128/jb.96.1.117-125.1968 · Cited by 40
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Mitchell, P. D. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80465-0 · Cited by 40
Electron Transport Phosphorylation
Baltscheffsky, H., & Baltscheffsky, M. (1974) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.43.070174.004255 · Cited by 40
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White, D. C. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97588-5 · Cited by 40
Formation of Methane from Serine by Cell-free Extracts of Methanobacillus omelianskii
Wood, J. M., Allam, A. M., Brill, W. J., & WOLFE, R. S. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96993-0 · Cited by 40
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Lara, F. J. S. (1959) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(59)90153-2 · Cited by 38
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Isolation of a Bisulfite Reductase Activity from Desulfotomaculum nigrificans and Its Identification as the Carbon Monoxide-Binding Pigment P582
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Bacterial reduction of tetrathionate
Pollock, M. R., & Knox, R. (1943) · Biochemical Journal · doi:10.1042/bj0370476 · Cited by 38
The Nutritional Requirements of Clostridium aceticum
Karlsson, J. L., Volcani, B. E., & Barker, H. A. (1948) · Journal of Bacteriology · doi:10.1128/jb.56.6.781-782.1948 · Cited by 37
20 Inorganic Pyrophosphatase of Escherichia coli
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Anaerobic degradation of lysine
Tsai, L., & Stadtman, T. C. (1968) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(68)90656-5 · Cited by 37
ACETYL PHOSPHATE FORMATION IN THE PHOSPHOROLYTIC CLEAVAGE OF PENTOSE PHOSPHATE
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Die Folsäure im Stoffwechsel der Einkohlenstoff‐Einheiten
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Characterization of the respiratory nitrate reductase of Klebsiella aerogenes as a molybdenum-containing iron-sulfur enzyme
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Involvement of a Membrane Potential in the Synthesis of ATP by Mitochondria
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The Redox Reactions in Propionic Acid Fermentation
Sone, N. (1972) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a129864 · Cited by 35
Structure of Rhodoquinone1
Moore, H. W., & Folkers, K. (1966) · Journal of the American Chemical Society · doi:10.1021/ja00955a032 · Cited by 35
The Physiological Role of Tetrathionate Respiration in Growing Citrobacter
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Purification and Properties of l-erythro-3,5-Diaminohexanoate Dehydrogenase from a Lysine-fermenting Clostridium
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Enzyme Complex Which Couples Glycerol-3-Phosphate Dehydrogenation to Fumarate Reduction in Escherichia coli
Miki, K., & Lin, E. C. C. (1973) · Journal of Bacteriology · doi:10.1128/jb.114.2.767-771.1973 · Cited by 34
Nitric Oxide-reducing Activity of Alcaligenes faecalis Cytochrome cd
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PRODUCTION AND UTILIZATION OF NITROUS OXIDE BY PSEUDOMONAS DENITRIFICANS
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Aldehyde Dehydrogenase
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Myokinase Equilibrium
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The selective action of tetrathionate in bacteriological media: A report to the medical research council
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Oxidative Phosphorylation Coupled with Nitrate Respiration
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Transport and Retention of K + and Other Metabolites in a Marine Pseudomonad and Their Relation to the Mechanism of Optical Effects
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Glyoxylate inhibition of clostridial pyruvate synthase
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Tightly bound adenine nucleotide in bacterial membrane ATPase
Abrams, A., Nolan, E. A., Jensen, C., & Smith, J. B. (1973) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(73)80054-3 · Cited by 33
Kinetics and properties of ?-ketothiolase from Clostridium pasteurianum
Berndt, H., & Schlegel, H. G. (1975) · Archives of Microbiology · doi:10.1007/bf00436325 · Cited by 33
Effect of enzymic assay conditions on sulfite reduction catalysed by desulfoviridin from Desulfovibrio gigas
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A propos des nitrate-réductases d'une bactérie dénitrifiante
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Phosphorylation coupled to NADH oxidation with fumarate in Streptococcus faecalis 10Cl
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The Metabolism of Malate and certain other Compounds by Desulphovibrio desulphuricans
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Alteration of fermentation products from butyrate to acetate by nitrate reduction in Clostridium perfringens
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Physiological and Chemical Properties of a Reductant-activated Inorganic Pyrophosphatase from Desulfovibrio desulfuricans
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ATP-dependent formation of methane from methylcobalamin by extracts of Methanobacillusomelianskii
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Evidence That apo-Reduced Nicotinamide Adenine Dinucleotide Dehydrogenase and apo-Electron-transferring Flavoprotein from Peptostreptococcus elsdenii Are Identical
Whitfield, C. D., & Mayhew, S. G. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42701-4 · Cited by 32
Menaquinone (MK-6) in the sulfate-reducing obligate anaerobe, Desulfovibrio
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Menaquinone-6 in the strict anaerobes DesulfovibriovulgarisandDesulfovibriogigas
Weber, M. M., Matschiner, J. T., & Peck, H. D. (1970) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(70)90696-0 · Cited by 31
Anaerobic Degradation of Lysine
Bray, R. C., & Stadtman, T. C. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99304-x · Cited by 31
A Transmembrane location for the proton‐translocating reduced ubiquinone→ nitrate reductase segment of the respiratory chain of Escherichia coli
Boxer, D. H., & CLEGG, R. A. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80417-0 · Cited by 31
Studies on Denitrification
Miyata, M., Matsubara, T., & Mori, T. (1969) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a129205 · Cited by 31
Biochemistry of Nitrate Respiration in Pseudomonas stutzeri I. Aerobic and Nitrate Respiration Routes of Carbohydrate Catabolism
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Equilibrium Constants of the Reactions of Acetyl Coenzyme A Synthetase and the Hydrolysis of Adenosine Triphosphate to Adenosine Monophosphate and Inorganic Pyrophosphate
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Formyltetrahydrofolate Synthetase
Joyce, B. K., & Himes, R. H. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96402-1 · Cited by 30
The Participation of Cytochromes in the Reduction of N2O to N2 by a Denitrifying Bacterium
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Ferredoxin-Dependent Conversion of Acetaldehyde to Acetate and H 2 in Extracts of S Organism
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Determination of steady-state concentrations of adenine nucleotides in growing C. kluyveri cells by biosynthetic labeling
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Purification and Properties of the Flavine-Stimulated Anaerobic l -α-Glycerophosphate Dehydrogenase ofEscherichia coli
Kistler, W. S., & Lin, E. C. C. (1972) · Journal of Bacteriology · doi:10.1128/jb.112.1.539-547.1972 · Cited by 30
[PHOSPHOTRANSACETYLASE FROM CLOSTRIDIUM KLUYVERI. CULTURE OF THE BACTERIUM, ISOLATION, CRYSTALLIZATION AND PROPERTIES OF THE ENZYME].
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INTERMEDIARY METABOLISM OF DIPLOCOCCUS GLYCINOPHILUS II
Klein, S. M., & Sagers, R. D. (1962) · Journal of Bacteriology · doi:10.1128/jb.83.1.121-126.1962 · Cited by 29
Total Synthesis of Acetate from CO 2 II. Purification and Properties of Formyltetrahydrofolate Synthetase from Clostridium thermoaceticum
Sun, A. Y., Ljungdahl, L. G., & Wood, H. G. (1969) · Journal of Bacteriology · doi:10.1128/jb.98.2.842-844.1969 · Cited by 28
Formyltetrahydrofolate Synthetase
Joyce, B. K., & Himes, R. H. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96403-3 · Cited by 28
21 Yeast and Other Inorganic Pyrophosphatases
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Biochemistry of Methane Formation
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Identification and Cobamide Coenzyme-dependent Formation of 3,5-Diaminohexanoic Acid, an Intermediate in Lysine Fermentation
Dekker, E. E., & Barker, H. A. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93298-9 · Cited by 28
FUMARATE REDUCTION AND ITS ROLE IN THE DIVERSION OF GLUCOSE FERMENTATION BY STREPTOCOCCUS FAECALIS
Deibel, R. H., & Kvetkas, M. J. (1964) · Journal of Bacteriology · doi:10.1128/jb.88.4.858-864.1964 · Cited by 28
Purification of acetokinase from Desulfovibrio desulfuricans.
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Solubilization and partial characterization of particulate dehydrogenases from Clostridium kluyveri
Hillmer, P., & Gottschalk, G. (1974) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(74)90146-6 · Cited by 28
[Fine structure of methanosarcina].
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Neuisolierung von Clostridium aceticum Wieringa und stoffwechselphysiologische Untersuchungen
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Dinitrophenol-Stimulated Adenosine Triphosphatase Activity in Extracts of Desulfovibrio gigas
Guarraia, L. J., & Peck, H. D. (1971) · Journal of Bacteriology · doi:10.1128/jb.106.3.890-895.1971 · Cited by 27
Particulate nature of enzymes involved in the fermentation of ethanol and acetate byClostridium kluyveri
Hillmer, P., & Gottschalk, G. (1972) · FEBS Letters · doi:10.1016/0014-5793(72)80200-x · Cited by 27
The metabolism of pyrimidines by proteolytic clostridia
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Studies on Soluble Cytochromes in Enterobacteriaceae :III. Localization of Cytochrome c -552 in the Surface Layer of Cells
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ACETATE, A KEY INTERMEDIATE IN METHANOGENESIS
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6 Ferredoxin-Linked Carboxylation Reactions
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Studies on Lysine-2,3-Aminomutase
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Starch Gel Electrophoresis of Fructose-6-Phosphate Phosphoketolase in the GenusBifidobacterium
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Oxidative Phosphorylation Coupled with Nitrate Respiration with Cell Free Extract of Pseudomonas denitrificans
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Mechanism of action of coenzyme B12. Hydrogen transfer in the isomerization of .beta.-methylaspartate to glutamate
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Electron transport function of a heat-stable protein and a flavoprotein in the oxidative decar☐ylation of glycine by Peptococcus glycinophilus
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Pyruvate formate lyase inRhodospirillum rubrum Ha adapted to anaerobic dark conditions
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An AMP-independent Sulphite Oxidase from Thiobacillus denitrificans: Purification and Properties
Aminuddin, M., & Nicholas, D. J. D. (1974) · Journal of General Microbiology · doi:10.1099/00221287-82-1-103 · Cited by 27
Solubilization and properties of formate dehydrogenases from the membrane of Escherichia coli
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Studies on Denitrification: VIII.* Production of Nitric Oxide by Denitrifying Reaction in the Presence of Tetramethyl-p-Phenylenediamine**
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Regulatory Properties of Acetokinase from Veillonella alcalescens
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NITRATE REDUCTASE IN CELL-FREE EXTRACTS OF A HAEMIN-REQUIRING STRAIN OF STAPHYLOCOCCUS AUREUS
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Thermodynamics and biology.
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Succinic Acid Production by Rumen Bacteria. III. Enzymic Studies on the Formation of Succinate by Ruminococcus Flavefaciens
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The breakdown of pyruvate by cell-free extracts of the rumen microorganism LC
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OXAMIC TRANSCARBAMYLASE OF STREPTOCOCCUS ALLANTOICUS
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Components Required for the Formation of CH4 from Methylcobalamin by Extracts of Methanobacillus omelianskii
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NAPHTHOQUINONE INTERMEDIATE IN THE RESPIRATION OF BACILLUS STEAROTHERMOPHILUS
Downey, R. J. (1962) · Journal of Bacteriology · doi:10.1128/jb.84.5.953-960.1962 · Cited by 26
Studies of the Acetate Kinase-Phosphotransacetylase and the Butanediol-Forming Systems in Aerobacter aerogenes
Brown, T. D. K., Pereira, C. R. S., & Størmer, F. C. (1972) · Journal of Bacteriology · doi:10.1128/jb.112.3.1106-1111.1972 · Cited by 26
Hydrogen Transfer between Substrates and Deoxyadenosylcobalamin in the Glutamate Mutase Reaction
Switzer, R. L., Baltimore, B. G., & Barker, H. A. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63655-5 · Cited by 25
The Relationship between Methane Production and Concentrations of Hydrogen in the Aqueous and Gaseous Phases during Rumen Fermentation in vitro
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Sagers, R. D., Benziman, M., & GUNSALUS, I. C. (1961) · Journal of Bacteriology · doi:10.1128/jb.82.2.233-238.1961 · Cited by 25
Requirement of Succinate for the Growth of Vibrio succinogenes
Niederman, R. A., & Wolin, M. J. (1972) · Journal of Bacteriology · doi:10.1128/jb.109.2.546-549.1972 · Cited by 25
Function of Ubiquinone in Electron Transport from Reduced Nicotinamide Adenine Dinucleotide to Nitrate and Oxygen in Aerobacter aerogenes
Knook, D. L., & Planta, R. J. (1971) · Journal of Bacteriology · doi:10.1128/jb.105.2.483-488.1971 · Cited by 25
Purification and some properties of the membrane‐bound respiratory nitrate reductase of Aerobacter aerogenes
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Partial purification of a dicyclohexylcarbodi-imide-sensitive membrane adenosine triphosphatase complex from the obligately anaerobic bacterium Clostridium Pasteurianum
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Standard free energy maps for the hydrolysis of ATP as a function of pH, pMg and pCa
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20. Phosphoenolpyruvate Synthetase and Pyruvate, Phosphate Dikinase
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Phosphotransacetylase from Clostridium acidiurici
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The Purple Membrane of Halobacterium halobium : A New System for Light Energy Conversion
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Demonstration of NADH-ferredoxin reductase in two saccharolytic clostridia
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Influence de la respiration anaérobie du nitrate et du fumarate sur le métabolisme fermentaire d'Aerobacter aerogenes
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Studies on the enzymic reduction of amino acids. V. Coupling of a DPNH-generating system to glycine reduction
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Functional anaerobic electron transport linked to the reduction of nitrate and fumarate in membranes from Escherichia coli as demonstrated by quenching of atebrin fluorescence
Haddock, B. A., & Kendall-Tobias, M. W. (1975) · Biochemical Journal · doi:10.1042/bj1520655 · Cited by 24
The participation of a ferredoxin of Clostridiumnigrificans in sulfite reduction
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Purification and Properties of Phosphotransacetylase from Veillonella alcalescens
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Energy Requirement for Microbial Growth
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Properties and function of clostridial membrane ATPase
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Role of Iron-Sulfur Proteins in Formate Metabolism
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Fumarate Reductase Activity ofStreptococcus faecalis
Aue, B. J., & Diebel, R. H. (1967) · Journal of Bacteriology · doi:10.1128/jb.93.6.1770-1776.1967 · Cited by 22
Terpenoid quinones of the anaerobic Propionibacterium shermanii
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CO 2 -DEPENDENT FERMENTATION OF GLUCOSE BY CYTOPHAGA SUCCINICANS
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The Role of Lipophilic Quinones in the Electron Transport System of Escherichia Coli*.
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Formation and Identification of 3-Keto-5-aminohexanoic Acid, a Probable Intermediate in Lysine Fermentation
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Electron-transport system of Vibrio succinogenes
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Phosphorolysis of carbamyl oxamic acid
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See all 4,146

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)
DOI: 10.1128/br.41.1.100-180.1977
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
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
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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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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Energy conservation in chemotrophic anaerobic bacteria

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About these checks