Interaction of ferredoxin with carbon monoxide dehydrogenase from Clostridium thermoaceticum.
作者： T Shanmugasundaram , H G Wood
DOI: 10.1016/S0021-9258(18)48368-8
关键词:
摘要: Acetogenic bacteria, as determined with Clostridium thermoaceticum, synthesize acetate by the acetyl-CoA pathway which involves reduction of CO2 to a methyl group and then combination CoA carbonyl formed from CO or (Wood, H.G., Ragsdale, S.W., Pezacka, E. (1986) Trends Biochem. Sci. 11, 14-18). Carbon monoxide dehydrogenase (CODH), key enzyme in this not only catalyzes oxidation but also final step, synthesis group, CO, CoA. Previously, it has been shown that ferredoxin can stimulate exchange CH3 14COSCoA (Ragsdale, Wood, H.G. (1985) J. Biol. Chem. 260, 3970-3977). In present study, observed CODH form an electrostatically stabilized complex. order identify binding region on CODH, were cross-linked using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide. The CODH-ferredoxin adduct was enzymatically active uncross-linked native complex subjected cyanogen bromide cleavage. By comparison high-performance liquid chromatography peptide profiles, mobility at least one is altered identified residues 229-239 alpha-subunit CODH.
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