Isolation of carbon monoxide dehydrogenase from Acetobacterium woodii and comparison of its properties with those of the Clostridium thermoaceticum enzyme
Open accessAbstract
An oxygen-labile carbon monoxide dehydrogenase was purified to at least 98% homogeneity from fructose-grown cells of Acetobacterium woodii. Gel filtration and electrophoresis experiments gave molecular weights of 480,000 and 153,000, respectively, of the active enzyme. The molecular weights for the subunits are 80,000 and 68,000; the subunits occur in equal proportion. The small subunit of the A. woodii enzyme differs in size from that of the Clostridium thermoaceticum enzyme; however, the large subunits are similar. The specific activity of the A. woodii enzyme, measured at 30 degrees C and pH 7.6, is 500 mumol of CO oxidized min-1 mg-1 with 20 mM methyl viologen as the electron acceptor. Analysis revealed (number per dimer) iron (9), acid-labile sulfide (12), nickel (1.4), and magnesium or zinc (1). This metal content is quite similar to that of the C. thermoaceticum enzyme (Ragsdale et al., J. Biol. Chem. 258:2364-2369, 1983). The nickel as well as the iron-sulfur clusters are redox-active, as was found for the C. thermoaceticum enzyme (Ragsdale et al., Biochem. Biophys. Res. Commun. 108:658-663, 1982). CO can reduce and CO2 can oxidize the iron-sulfur clusters. The enzyme is inhibited by cyanide, but CO2 in the presence of reduced methyl viologen or CO alone can reverse or prevent this inhibition. Several ferredoxins, flavodoxin, and rubredoxin and some artificial electron carriers were tested for their relative rates of reaction with the CO dehydrogenases from A. woodii, C. thermoaceticum, and Clostridium formicoaceticum. Rubredoxin was by far the most reactive acceptor and is proposed to be the primary natural electron carrier for the acetogenic CO dehydrogenases.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Cyanide binds to CODH, a key enzyme of the Wood-Ljungdahl pathway.
“Cyanide binds to CODH (Ragsdale et al., 1983), a key enzyme of the WLP.”
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 Ragsdale et al., 1983
Cites
DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS *
Davis, B. J. (1964) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1964.tb14213.x · Cited by 16,129 · see citing works
Data Reduction and Error Analysis for the Physical Sciences
Bevington, P. R., Robinson, D. K., Blair, J. M., Mallinckrodt, A. J., & McKay, S. R. (1993) · Computers in Physics · doi:10.1063/1.4823194 · Cited by 14,992 · see citing works
Estimation of the molecular weights of proteins by Sephadex gel-filtration
Andrews, P. (1964) · Biochemical Journal · doi:10.1042/bj0910222 · Cited by 3,903 · see citing works
Hedrick, J. L., & Smith, A. J. (1968) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(68)90569-9 · Cited by 1,901 · see citing works
[1] Measurement of molecular weights by electrophoresis on SDS-acrylamide gel
Weber, K., Pringle, J. R., & Osborn, M. (1972) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(72)26003-7 · Cited by 1,723 · see citing works
Reisner, A. H., Nemes, P., & Bucholtz, C. A. (1975) · Analytical Biochemistry · doi:10.1016/0003-2697(75)90461-3 · Cited by 618 · see citing works
[39] Analytical disc gel electrophoresis
Gabriel, O. (1971) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(71)22041-3 · Cited by 493 · see citing works
Acetobacterium, a New Genus of Hydrogen-Oxidizing, Carbon Dioxide-Reducing, Anaerobic Bacteria
Balch, W. E., Schoberth, S. M., Tanner, R. S., & WOLFE, R. S. (1977) · International Journal of Systematic Bacteriology · doi:10.1099/00207713-27-4-355 · Cited by 422 · see citing works
Yamamoto, I., Saiki, T., Liu, S. M., & Ljungdahl, L. G. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33062-x · Cited by 276 · see citing works
Self-citationCarbon Monoxide Oxidation by Clostridium thermoaceticum and Clostridium formicoaceticum
Diekert, G. B., & Thauer, R. K. (1978) · Journal of Bacteriology · doi:10.1128/jb.136.2.597-606.1978 · Cited by 257 · see citing works
Ragsdale, S. W., Clark, J. E., Ljungdahl, L. G., Lundie, L. L., & Drake, H. L. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32932-6 · Cited by 235 · see citing works
Uffen, R. L. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.9.3298 · Cited by 231 · see citing works
Rubredoxin: a new electron transfer protein from Clostridium pasteurianum.
Lovenberg, W. M., & Sobel, B. E. (1965) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.54.1.193 · Cited by 223 · see citing works
Elemental analysis of soil extracts and plant tissue ash by plasma emission spectroscopy
Jones, J. B. (1977) · Communications in Soil Science and Plant Analysis · doi:10.1080/00103627709366727 · Cited by 202 · see citing works
Function of reduced pyridine nucleotide-ferredoxin oxidoreductases in saccharolytic Clostridia
Jungermann, K. A., Thauer, R. K., Leimenstoll, G., & Decker, K. (1973) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(73)90175-8 · Cited by 192 · see citing works
Drake, H. L., Hu, S. I., & Wood, H. G. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68568-6 · Cited by 165 · see citing works
Purification of carbon monoxide dehydrogenase, a nickel enzyme from Clostridium thermocaceticum.
Drake, H. L., Hu, S. I., & Wood, H. G. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)79682-1 · Cited by 151 · see citing works
Andreesen, J. R., Gottschalk, G., & Schlegel, H. G. (1970) · Archives of Microbiology · doi:10.1007/bf00409521 · Cited by 150 · see citing works
Simplified methods for the estimation of iron in mitochondria and submitochondrial fractions
DOEG, K. A., & Ziegler, D. M. (1962) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(62)90041-3 · Cited by 145 · see citing works
Carbon monoxide metabolism of the methylotrophic acidogen Butyribacterium methylotrophicum
Lynd, L. H., Kerby, R. L., & Zeikus, J. G. (1982) · Journal of Bacteriology · doi:10.1128/jb.149.1.255-263.1982 · Cited by 142 · see citing works
Hu, S. I., Drake, H. L., & Wood, H. G. (1982) · Journal of Bacteriology · doi:10.1128/jb.149.2.440-448.1982 · Cited by 125 · see citing works
The inactivation of yeast enolase by 2,3-butanedione
Elliott, J. I., & Brewer, J. M. (1978) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(78)90285-0 · Cited by 119 · see citing works
The Mechanism of Action of Ethanolamine Ammonia-Lyase, a B12-dependent Enzyme
BABIOR, B. M., Moss, T. H., Orme‐Johnson, W. H., & Beinert, H. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42452-6 · Cited by 110 · see citing works
[39] Formate dehydrogenase, a selenium-tungsten enzyme from Clostridium thermoaceticum
Ljungdahl, L. G., & Andreesen, J. R. (1978) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(78)53042-5 · Cited by 103 · see citing works
Unambiguous identification of the nickel EPR signal in 61Ni-enriched Desulfovibrio gigas hydrogenase
Moura, J. J. G., Moura, I., Huynh, B. H., Krüger, H., Teixeira, M. S., DuVarney, R. C., DerVartanian, D. V., Xavier, A. V., Peck, H. D., & LeGall, J. (1982) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(82)80060-0 · Cited by 103 · see citing works
Meyer, O. O. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68196-2 · Cited by 98 · see citing works
Kojima, N., Fox, J. A., Hausinger, R. P., Daniels, L., Orme‐Johnson, W. H., & Walsh, C. T. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.2.378 · Cited by 93 · see citing works
Evidence for nickel and a three-iron center in the hydrogenase of Desulfovibrio desulfuricans.
Krüger, H., Huynh, B. H., Ljungdahl, P. O., Xavier, A. V., DerVartanian, D. V., Moura, I., Peck, H. D., Teixeira, M. S., Moura, J. J. G., & LeGall, J. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33323-4 · Cited by 92 · see citing works
Ragsdale, S. W., Ljungdahl, L. G., & DerVartanian, D. V. (1982) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(82)90880-4 · Cited by 90 · see citing works
Electrophoresis and electrofocusing on polyacrylamide gel in the study of native macromolecules
Chrambach, A. (1980) · Molecular and Cellular Biochemistry · doi:10.1007/bf00230953 · Cited by 75 · see citing works
Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans
Meyer, O. O., & Schlegel, H. G. (1980) · Journal of Bacteriology · doi:10.1128/jb.141.1.74-80.1980 · Cited by 74 · see citing works
[30] Analysis of acid-labile sulfide and sulfhydryl groups
Rabinowitz, J. C. (1978) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(78)53033-4 · Cited by 67 · see citing works
Moore, M. R., O’Brien, W. E., & Ljungdahl, L. G. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42355-7 · Cited by 66 · see citing works
Diekert, G. B., & Thauer, R. K. (1980) · FEMS Microbiology Letters · doi:10.1111/j.1574-6941.1980.tb01622.x · Cited by 65 · see citing works
A four-iron, four-sulfide ferredoxin with high thermostability from Clostridium thermoaceticum
Yang, S., Ljungdahl, L. G., & LeGall, J. (1977) · Journal of Bacteriology · doi:10.1128/jb.130.3.1084-1090.1977 · Cited by 65 · see citing works
Kim, Y. M., & Hegeman, G. D. (1981) · Journal of Bacteriology · doi:10.1128/jb.148.3.904-911.1981 · Cited by 64 · see citing works
Drake, H. L. (1982) · Journal of Bacteriology · doi:10.1128/jb.149.2.561-566.1982 · Cited by 63 · see citing works
Carbon Monoxide Oxidation by Growing Cultures of Clostridium pasteurianum
Fuchs, G., SCHNITKER, U., & Thauer, R. K. (1974) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1974.tb03816.x · Cited by 59 · see citing works
Oxidation of Carbon Monoxide in Cell Extracts of Pseudomonas carboxydovorans
Meyer, O. O., & Schlegel, H. G. (1979) · Journal of Bacteriology · doi:10.1128/jb.137.2.811-817.1979 · Cited by 52 · see citing works
Levels of enzymes involved in the synthesis of acetate from CO2 in Clostridium thermoautotrophicum
Clark, J. E., Ragsdale, S. W., Ljungdahl, L. G., & Wiegel, J. (1982) · Journal of Bacteriology · doi:10.1128/jb.151.1.507-509.1982 · Cited by 49 · see citing works
Elliott, J. I., & Ljungdahl, L. G. (1982) · Journal of Bacteriology · doi:10.1128/jb.151.1.328-333.1982 · Cited by 46 · see citing works
Clark, J. E., & Ljungdahl, L. G. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34857-9 · Cited by 45 · see citing works
Isolation and properties of reduced nicotinamide adenine dinucleotide-rubredoxin oxidoreductase of
Petitdemange, H., Marczak, R., Blusson, H., & Gay, R. (1979) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(79)91202-6 · Cited by 42 · see citing works
The Mechanism of Action of Ethanolamine Ammonia-Lyase, a B12-dependent Enzyme
Carty, T. J., BABIOR, B. M., & Abeles, R. H. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61790-9 · Cited by 42 · see citing works
Nickel requirement of Acetobacterium woodii
Diekert, G. B., & Ritter, M. (1982) · Journal of Bacteriology · doi:10.1128/jb.151.2.1043-1045.1982 · Cited by 38 · see citing works
THOMSON, A. J. (1982) · Nature · doi:10.1038/298602a0 · Cited by 31 · see citing works
[59] Purification of electron-transfer components from sulfate-reducing bacteria
Gall, J. L., & Forget, N. (1978) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(78)53062-0 · Cited by 25 · see citing works
Determination of hydrogenase activity using an anaerobic spectrophotometric device
Fernández, V. M., Gutiérrez, C., & Ballesteros, A. O. (1982) · Analytical Biochemistry · doi:10.1016/0003-2697(82)90320-7 · Cited by 22 · see citing works
Electron transport system of an aerobic carbon monoxide-oxidizing bacterium
Kim, Y. M., & Hegeman, G. D. (1981) · Journal of Bacteriology · doi:10.1128/jb.148.3.991-994.1981 · Cited by 18 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Acetogenesis and the Wood–Ljungdahl pathway of CO2 fixation
Ragsdale, S. W., & Pierce, E. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.08.012 · Cited by 1,337 · see citing works
Schuchmann, K., & Müller, V. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3365 · Cited by 845 · see citing works
The Autotrophic Pathway of Acetate Synthesis in Acetogenic Bacteria
Ljungdhal, L. G. (1986) · Annual Review of Microbiology · doi:10.1146/annurev.mi.40.100186.002215 · Cited by 575 · see citing works
Liew, F., Martin, M. E., Tappel, R. C., Heijstra, B. D., Mihalcea, C., & Köpke, M. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00694 · Cited by 485 · see citing works
Methanogens and the diversity of archaebacteria
Jones, W. J., Nagle, D. P., & Whitman, W. B. (1987) · Microbiological Reviews · doi:10.1128/mr.51.1.135-177.1987 · Cited by 464 · see citing works
Nickel-Containing Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase,
Ragsdale, S. W., & Kumar, M. (1996) · Chemical Reviews · doi:10.1021/cr950058+ · Cited by 331 · see citing works
Nickel utilization by microorganisms
Hausinger, R. P. (1987) · Microbiological Reviews · doi:10.1128/mr.51.1.22-42.1987 · Cited by 292 · see citing works
CO2 fixation in acetogenic bacteria: Variations on a theme
Fuchs, G. (1986) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1986.tb01859.x · Cited by 294 · see citing works
The three classes of hydrogenases from sulfate-reducing bacteria of the genus Desulfovibrio
Fauque, G. D., Peck, H. D., Moura, J. J. G., Huynh, B. H., Berlier, Y. M., DerVartanian, D. V., Teixeira, M. S., Przybyla, A., Lespinat, P. A., Moura, I., et al. (1988) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1988.tb02748.x · Cited by 279 · see citing works
Essential Roles and Hazardous Effects of Nickel in Plants
Ahmad, M. S. A., & Ashraf, M. (2011) · Reviews of Environmental Contamination and Toxicology · doi:10.1007/978-1-4614-0668-6_6 · Cited by 257 · see citing works
Enzymology of the Acetyl-CoA Pathway of CO2Fixation
Ragsdale, S. W. (1991) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239109114070 · Cited by 259 · see citing works
Ragsdale, S. W., & Wood, H. G. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89217-1 · Cited by 249 · see citing works
Carbon monoxide-dependent energy metabolism in anaerobic bacteria and archaea
Oelgeschläger, E., & Rother, M. (2008) · Archives of Microbiology · doi:10.1007/s00203-008-0382-6 · Cited by 236 · see citing works
Diekert, G. B., & Wohlfarth, G. (1994) · Antonie van Leeuwenhoek · doi:10.1007/bf00871640 · Cited by 226 · see citing works
Svetlitchnyi, V. A., Peschel, C., Acker, G., & Meyer, O. O. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.17.5134-5144.2001 · Cited by 223 · see citing works
The acetyl-CoA pathway of autotrophic growth
Wood, H. G., Ragsdale, S. W., & Pezacka, E. H. (1986) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1986.tb01865.x · Cited by 214 · see citing works
Bacterial synthesis gas (syngas) fermentation
Bengelsdorf, F. R., Straub, M., & Dürre, P. (2013) · Environmental Technology · doi:10.1080/09593330.2013.827747 · Cited by 211 · see citing works
Genetics and Biochemistry of Clostridium Relevant to Development of Fermentation Processes
Rogers, P. (1986) · Advances in applied microbiology · doi:10.1016/s0065-2164(08)70438-6 · Cited by 176 · see citing works
CO2 photoreduction at enzyme-modified metal oxide nanoparticles
Woolerton, T. W., Sheard, S., Pierce, E., Ragsdale, S. W., & Armstrong, F. A. (2011) · Energy & Environmental Science · doi:10.1039/c0ee00780c · Cited by 176 · see citing works
Bacterial Anaerobic Synthesis Gas (Syngas) and CO 2 + H 2 Fermentation
Bengelsdorf, F. R., Beck, M. H., Erz, C., Hoffmeister, S., Karl, M. M., Riegler, P., Wirth, S., Poehlein, A., Weuster‐Botz, D., & Dürre, P. (2018) · Advances in applied microbiology · doi:10.1016/bs.aambs.2018.01.002 · Cited by 164 · see citing works
Hess, V., Schuchmann, K., & Müller, V. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.510255 · Cited by 157 · see citing works
Terlesky, K. C., Nelson, M. J., & Ferry, J. G. (1986) · Journal of Bacteriology · doi:10.1128/jb.168.3.1053-1058.1986 · Cited by 153 · see citing works
Ragsdale, S. W., Wood, H. G., & Antholine, W. E. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.20.6811 · Cited by 152 · see citing works
Lindahl, P. A., Münck, E., & Ragsdale, S. W. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39675-9 · Cited by 138 · see citing works
CO Metabolism in the Acetogen Acetobacterium woodii
Bertsch, J., & Müller, V. (2015) · Applied and Environmental Microbiology · doi:10.1128/aem.01772-15 · Cited by 134 · see citing works
Gomes, C. M., Silva, G. P. D. L., Oliveira, S., LeGall, J., Liu, M., Xavier, A. V., Rodrigues‐Pousada, C., & Teixeira, M. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.36.22502 · Cited by 133 · see citing works
Doukov, T. I., Blasiak, L. C., Seravalli, J., Ragsdale, S. W., & Drennan, C. L. (2008) · Biochemistry · doi:10.1021/bi702386t · Cited by 128 · see citing works
Single-Carbon Chemistry of Acetogenic and Methanogenic Bacteria
Zeikus, J. G., Kerby, R. L., & Krzycki, J. A. (1985) · Science · doi:10.1126/science.3919443 · Cited by 127 · see citing works
The acetyl-CoA pathway: a newly discovered pathway of autotrophic growth
Wood, H. G., Ragsdale, S. W., & Pezacka, E. H. (1986) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(86)90223-9 · Cited by 118 · see citing works
Watt, R. K., & Ludden, P. W. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050456 · Cited by 116 · see citing works
Characterization and purification of carbon monoxide dehydrogenase from Methanosarcina barkeri
Krzycki, J. A., & Zeikus, J. G. (1984) · Journal of Bacteriology · doi:10.1128/jb.158.1.231-237.1984 · Cited by 113 · see citing works
Electron transfer reactions in methanogens
Keltjens, J. T., & van der DRIFT, C. (1986) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1986.tb01862.x · Cited by 112 · see citing works
Mössbauer study of CO dehydrogenase from Clostridium thermoaceticum.
Lindahl, P. A., Ragsdale, S. W., & Münck, E. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39676-0 · Cited by 111 · see citing works
Liang, C. H. E. N., Liu, M., LeGall, J., Fareleira, P., Santos, H., & Xavier, A. V. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18162.x · Cited by 95 · see citing works
Gas fermentation: cellular engineering possibilities and scale up
Heijstra, B. D., Leang, C., & Juminaga, A. (2017) · Microbial Cell Factories · doi:10.1186/s12934-017-0676-y · Cited by 92 · see citing works
Clark, J. E., & Ljungdahl, L. G. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90590-9 · Cited by 87 · see citing works
Involvement of Ech hydrogenase in energy conservation of Methanosarcina mazei
Welte, C. U., Krätzer, C., & Deppenmeier, U. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07744.x · Cited by 87 · see citing works
Hu, S. I., Pezacka, E. H., & Wood, H. G. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)47238-3 · Cited by 85 · see citing works
Kung, Y., Doukov, T. I., Seravalli, J., Ragsdale, S. W., & Drennan, C. L. (2009) · Biochemistry · doi:10.1021/bi900574h · Cited by 79 · see citing works
[14] Rubredoxin in crystalline state
Sieker, L. C., Stenkamp, R. E., & LeGall, J. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(94)43016-0 · Cited by 79 · see citing works
Hess, V., Poehlein, A., Schoelmerich, M. C., Daniel, R., & Müller, V. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-1139 · Cited by 75 · see citing works
Das, A., Coulter, E. D., Kurtz, D. M. J., & Ljungdahl, L. G. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.5.1560-1567.2001 · Cited by 74 · see citing works
Ensign, S. A., Hyman, M. R., & Ludden, P. W. (1989) · Biochemistry · doi:10.1021/bi00438a011 · Cited by 72 · see citing works
Pezacka, E. H., & Wood, H. G. (1984) · Archives of Microbiology · doi:10.1007/bf00425809 · Cited by 68 · see citing works
Grahame, D. A., & Stadtman, T. C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61412-7 · Cited by 69 · see citing works
The Evolution of Acetyl-CoA Synthase
Lindahl, P. A., & Chang, B. S. W. (2001) · Origins of Life and Evolution of Biospheres · doi:10.1023/a:1011809430237 · Cited by 67 · see citing works
Yoon, K.-S., Hille, R., Hemann, C. F., & Tabita, F. R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.42.29772 · Cited by 67 · see citing works
Calderon, R. H., García‐Cerdán, J. G., Malnoë, A., Cook, R., Russell, J. J., Gaw, C., Dent, R. M., de Vitry, C., & Niyogi, K. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.487629 · Cited by 67 · see citing works
Novel Iron—Sulfur Centers in Metalloenzymes and Redox Proteins from Extremely Thermophilic Bacteria
Adams, M. W. W. (1992) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60068-9 · Cited by 67 · see citing works
Role of carbon monoxide dehydrogenase in the autotrophic pathway used by acetogenic bacteria.
Pezacka, E. H., & Wood, H. G. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.20.6261 · Cited by 66 · see citing works
Oehler, D., Poehlein, A., Leimbach, A., Müller, N., Daniel, R., Gottschalk, G., & Schink, B. (2012) · BMC Genomics · doi:10.1186/1471-2164-13-723 · Cited by 64 · see citing works
Nickel–Iron–Sulfur Active Sites: Hydrogenase and Co Dehydrogenase
Fontecilla-Camps, J. C., & Ragsdale, S. W. (1999) · Advances in inorganic chemistry · doi:10.1016/s0898-8838(08)60081-1 · Cited by 64 · see citing works
Gadkari, D., Schricker, K., Acker, G., Kroppenstedt, R. M., & Meyer, O. O. (1990) · Applied and Environmental Microbiology · doi:10.1128/aem.56.12.3727-3734.1990 · Cited by 62 · see citing works
Ensign, S. A., Bonam, D., & Ludden, P. W. (1989) · Biochemistry · doi:10.1021/bi00438a010 · Cited by 60 · see citing works
The autotrophic pathway of acetogenic bacteria. Role of CO dehydrogenase disulfide reductase.
Pezacka, E. H., & Wood, H. G. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35983-5 · Cited by 59 · see citing works
Im, C. H., Kim, C., Song, Y. E., Oh, S., Jeon, B., & Kim, J. R. (2017) · Chemosphere · doi:10.1016/j.chemosphere.2017.10.004 · Cited by 57 · see citing works
Hydrogenase from Acetobacterium woodii
Ragsdale, S. W., & Ljungdahl, L. G. (1984) · Archives of Microbiology · doi:10.1007/bf00408380 · Cited by 57 · see citing works
Turner, A. P. F., Aston, W. J., Higgins, I. J., Bell, J., Colby, J., Davis, G. B., & Hill, H. A. O. (1984) · Analytica Chimica Acta · doi:10.1016/s0003-2670(00)81505-6 · Cited by 57 · see citing works
Roberts, D. L., James-Hagstrom, J. E., Garvin, D. K., Gorst, C. M., Runquist, J. A., Baur, J. R., Haase, F. C., & Ragsdale, S. W. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.1.32 · Cited by 56 · see citing works
Novak, K., Neuendorf, C. S., Kofler, I., Kieberger, N., Klamt, S., & Pflügl, S. (2020) · Bioresource Technology · doi:10.1016/j.biortech.2020.124573 · Cited by 54 · see citing works
The pyruvate:ferredoxin oxidoreductase of the thermophilic acetogen, Thermoanaerobacter kivui
Katsyv, A., Schoelmerich, M. C., Basen, M., & Müller, V. (2021) · FEBS Open Bio · doi:10.1002/2211-5463.13136 · Cited by 54 · see citing works
CO2-Fixation Strategies in Energy Extremophiles: What Can We Learn From Acetogens?
Lemaire, O. N., Jespersen, M., & Wagner, T. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00486 · Cited by 52 · see citing works
Welte, C. U., Kallnik, V., Grapp, M., Bender, G., Ragsdale, S. W., & Deppenmeier, U. (2009) · Journal of Bacteriology · doi:10.1128/jb.01307-09 · Cited by 52 · see citing works
Lemaire, O. N., & Wagner, T. (2020) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2020.148330 · Cited by 47 · see citing works
Paramagnetic centers of carbon monoxide dehydrogenase from aceticlastic Methanosarcina barkeri
Krzycki, J. A., Mortenson, L. E., & Prince, R. C. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83223-9 · Cited by 52 · see citing works
Evidence That Carbon Monoxide Is an Obligatory Intermediate in Anaerobic Acetyl-CoA Synthesis
Menon, S., & Ragsdale, S. W. (1996) · Biochemistry · doi:10.1021/bi961014d · Cited by 51 · see citing works
Ragsdale, S. W., & Ljungdahl, L. G. (1984) · Journal of Bacteriology · doi:10.1128/jb.157.1.1-6.1984 · Cited by 51 · see citing works
Structure, function and distribution of soluble bacterial redox proteins
Meyer, T. E., & Cusanovich, M. A. (1989) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(89)80196-3 · Cited by 50 · see citing works
Jetten, M. S. M., Stams, A. J. M., & Zehnder, A. J. B. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb14744.x · Cited by 49 · see citing works
Metabolic response of Clostridium ljungdahlii to oxygen exposure
Whitham, J. M., Tirado-Acevedo, O., Chinn, M. S., Pawlak, J. J., & Grunden, A. M. (2015) · Applied and Environmental Microbiology · doi:10.1128/aem.02491-15 · Cited by 47 · see citing works
Ma, K., & Adams, M. W. W. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.17.5530-5533.1999 · Cited by 47 · see citing works
O2-tolerant CO dehydrogenase via tunnel redesign for the removal of CO from industrial flue gas
Kim, S. M., Lee, J., Kang, S. H., Heo, Y., Yoon, H., Hahn, J., Lee, H. H., & Kim, Y. H. (2022) · Nature Catalysis · doi:10.1038/s41929-022-00834-y · Cited by 46 · see citing works
Welte, C. U., & Deppenmeier, U. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08048.x · Cited by 46 · see citing works
Cohen, S. E., Can, M., Wittenborn, E. C., Hendrickson, R. A., Ragsdale, S. W., & Drennan, C. L. (2020) · ACS Catalysis · doi:10.1021/acscatal.0c03033 · Cited by 43 · see citing works
Jetten, M. S. M., Hagen, W. R., Pierik, A. J., Stams, A. J. M., & Zehnder, A. J. B. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb15717.x · Cited by 44 · see citing works
Tan, G. O., Ensign, S. A., Ciurli, S., Scott, M. J., Hedman, B., Holm, R. H., Ludden, P. W., Korszun, Z. R., Stephens, P. J., & Hodgson, K. O. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.10.4427 · Cited by 43 · see citing works
Hashsham, S. A., & Freedman, D. L. (1999) · Applied and Environmental Microbiology · doi:10.1128/aem.65.10.4537-4542.1999 · Cited by 42 · see citing works
A novel way to utilize hydrogen and carbon dioxide in acidogenic reactor through homoacetogenesis
Yan, B. H., Selvam, A., Xu, S. Y., & Wong, J. W. C. (2014) · Bioresource Technology · doi:10.1016/j.biortech.2014.02.014 · Cited by 41 · see citing works
Acetogenic and Acid-Producing Clostridia
Ljungdahl, L. G., Hugenholtz, J., & Wiegel, J. (1989) · Springer eBooks · doi:10.1007/978-1-4757-9718-3_5 · Cited by 41 · see citing works
Rey, L. C., Hidalgo, E., Palacios, J. M., & Ruiz‐Argüeso, T. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90886-o · Cited by 39 · see citing works
Growth and Product Formation of Clostridium ljungdahlii in Presence of Cyanide
Oswald, F., Zwick, M., Omar, O., Hotz, E. N., & Neumann, A. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01213 · Cited by 36 · see citing works
Shanmugasundaram, T., Kumar, G. K., & Wood, H. G. (1988) · Biochemistry · doi:10.1021/bi00417a045 · Cited by 36 · see citing works
Amino acid sequence and function of rebredoxin from Desulfovibrio vulgaris Miyazaki
Shimizu, F., Ogata, M., Yagi, T., Wakabayashi, S., & Matsubara, H. (1989) · Biochimie · doi:10.1016/0300-9084(89)90020-5 · Cited by 35 · see citing works
Fritsch, J., Lenz, O., & Friedrich, B. (2011) · Journal of Bacteriology · doi:10.1128/jb.01427-10 · Cited by 34 · see citing works
Proton Translocation in Methanogens
Welte, C. U., & Deppenmeier, U. (2011) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-385112-3.00013-5 · Cited by 34 · see citing works
Jain, S., Katsyv, A., Basen, M., & Müller, V. (2021) · Extremophiles · doi:10.1007/s00792-021-01251-y · Cited by 33 · see citing works
Seravalli, J., Zhao, S., & Ragsdale, S. W. (1999) · Biochemistry · doi:10.1021/bi982473c · Cited by 33 · see citing works
Maiti, B. K., Almeida, R. M., Moura, I., & Moura, J. J. G. (2017) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2017.10.001 · Cited by 35 · see citing works
Crystal structure of rubredoxin from Desulfovibrio gigas to ultra-high 0.68Å resolution
Chen, C., Lin, Y.-H., Huang, Y., & Liu, M. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.07.205 · Cited by 33 · see citing works
Schwarz, F. M., Ciurus, S., Jain, S., Baum, C., Wiechmann, A., Basen, M., & Müller, V. (2020) · Microbial Biotechnology · doi:10.1111/1751-7915.13663 · Cited by 32 · see citing works
Purification and properties of carbon monoxide dehydrogenase from Methanococcus vannielii
DeMoll, E., Grahame, D. A., Harnly, J. M., Tsai, L., & Stadtman, T. C. (1987) · Journal of Bacteriology · doi:10.1128/jb.169.9.3916-3920.1987 · Cited by 32 · see citing works
Energetics of Acetogenesis from C1 Units
Diekert, G. B., & Wohlfarth, G. (1994) · Springer eBooks · doi:10.1007/978-1-4615-1777-1_5 · Cited by 31 · see citing works
Ragsdale, S. W. (1994) · Springer eBooks · doi:10.1007/978-1-4615-1777-1_3 · Cited by 29 · see citing works
Chen, J. C., & Mortenson, L. E. (1992) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(92)90111-c · Cited by 29 · see citing works
Prince, C., & Jia, Z. (2015) · Structure · doi:10.1016/j.str.2015.06.011 · Cited by 26 · see citing works
Hyeon, J. E., Kim, S. W., Park, C., & Han, S. O. (2015) · Chemical Communications · doi:10.1039/c5cc00832h · Cited by 26 · see citing works
Lu, W. P., Jablonski, P. E., Rasche, M. E., Ferry, J. G., & Ragsdale, S. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36944-2 · Cited by 24 · see citing works
da Costa, P. N., Romão, C. V., LeGall, J., Xavier, A. V., Melo, E. C. C., Teixeira, M. S., & Saraiva, L. M. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02509.x · Cited by 24 · see citing works
Kitamura, M., Koshino, Y., Kamikawa, Y., Kohno, K., Kojima, S., Miura, K., Sagara, T., Akutsu, H., Kumagai, I., & Nakaya, T. (1997) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(96)00203-5 · Cited by 23 · see citing works
Carbonyl sulfide inhibition of CO dehydrogenase from Rhodospirillum rubrum
Hyman, M. R., Ensign, S. A., Arp, D. J., & Ludden, P. W. (1989) · Biochemistry · doi:10.1021/bi00443a007 · Cited by 23 · see citing works
- Authors
- Ragsdale, S. W., Ljungdahl, L. G., & DerVartanian, D. V.
- Affiliations
- University of Georgia (US)
- ORCID
- Ragsdale, S W
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 1983-09
- Volume
- 155
- Issue
- 3
- Pages
- 1224-1237
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC217820
- OpenAlex
- W1766118319
- Cited by
- 145
- References
- 49
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 5 · 2023: 2 · 2022: 4 · 2021: 2 · 2020: 8 · 2018: 2 · 2017: 4 · 2016: 1 · 2015: 4 · 2014: 5 · 2013: 3 · 2012: 1
- FWCI
- 17.03
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Bacteriology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
- Physical Sciences › Engineering › Building and Construction › Anaerobic Digestion and Biogas Production
- Keywords
- carbon monoxide dehydrogenase, Acetobacterium woodii, Clostridium thermoaceticum, enzyme purification, enzyme subunit structure, metal content, iron-sulfur clusters, cyanide inhibition, electron carriers, rubredoxin, acetogenic bacteria, paraquat
- MeSH terms
- Aldehyde Oxidoreductases, Clostridium, Electron Spin Resonance Spectroscopy, Ferredoxins, Formates, Gram-Positive Bacteria, Kinetics, Metals, Molecular Weight, Multienzyme Complexes, Oxidation-Reduction, Potassium Cyanide, Rubredoxins, Spectrum Analysis
About these checks
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 ›
Are you an author, or do you see a problem with this page? Request a review