Acetate biosynthesis by acetogenic bacteria. Evidence that carbon monoxide dehydrogenase is the condensing enzyme that catalyzes the final steps of the synthesis.
Open Access
- 1 April 1985
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 260 (7), 3970-3977
- https://doi.org/10.1016/s0021-9258(18)89217-1
Abstract
No abstract availableThis publication has 27 references indexed in Scilit:
- 13C and 61Ni isotope substitutions confirm the presence of a nickel(III)-carbon species in acetogenic CO dehydrogenasesBiochemical and Biophysical Research Communications, 1983
- ESR characteristics of sulphydryl-containing peptide-nickel(III) complexes: Implication for nickel(III) center of hydrogenasesBiochemical and Biophysical Research Communications, 1983
- Mechanistic Pathways in the Catalytic Carbonylation of Methanol by Rhodium and Iridium ComplexesPublished by Elsevier ,1979
- The inactivation of yeast enolase by 2,3-butanedioneArchives of Biochemistry and Biophysics, 1978
- [39] Formate dehydrogenase, a selenium-tungsten enzyme from Clostridium thermoaceticumMethods in Enzymology, 1978
- The use of Coomassie Brilliant Blue G250 perchloric acid solution for staining in electrophoresis and isoelectric focusing on polyacrylamide gelsAnalytical Biochemistry, 1975
- Functional arginyl residues as NADH binding sites of alcohol dehydrogenasesBiochemistry, 1974
- Functional arginyl residues in carboxypeptidase A. Modification with butanedioneBiochemistry, 1973
- Determination and degradation of microquantities of acetateAnalytical Biochemistry, 1971
- PREPARATION OF ACETYL COENZYME A1Journal of the American Chemical Society, 1952