The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
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.
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“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
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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
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 15,003
Estimation of the molecular weights of proteins by Sephadex gel-filtration
Andrews, P. (1964) · Biochemical Journal · doi:10.1042/bj0910222 · Cited by 3,903
Hedrick, J. L., & Smith, A. J. (1968) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(68)90569-9 · Cited by 1,901
[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
Reisner, A. H., Nemes, P., & Bucholtz, C. A. (1975) · Analytical Biochemistry · doi:10.1016/0003-2697(75)90461-3 · Cited by 618
[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
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
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
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
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Research works printed but not linked: 1
- Ljungdahl L. G. and H. G. Wood. 1982. Acetate biosynthesis p. 166-202. In D. Dolphin (ed.) B12 vol. 2. John Wiley & Sons Inc. New York.
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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 1,409
Schuchmann, K., & Müller, V. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3365 · Cited by 845
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
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
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
Metadata
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › 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
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