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- W2094657311 abstract "The structure of carbon monoxide dehydrogenase/acetyl-coenzyme A synthase (CODH/ACS), a central enzyme in the anaerobic metabolism of acetyl-coenzyme A (acetyl-CoA), has been solved to a resolution of 2.2A. The active-site metal cluster responsible for catalyzing acetyl C-C bond synthesis and cleavage, designated the A center, was identified as an Fe(4)S(4) iron sulfur cluster with one of its cysteine thiolates acting as a bridge to an adjacent binuclear metal site. Nickel was found at one position in the binuclear site and the other metal was indicated to be copper - a surprising result, implying a previously unrecognized role for copper. Details of the A center provided new insight into the unusual organometallic mechanism of acetyl C-C bond formation and cleavage, with substantial conformational changes indicated for binding of the large methylcorrinoid protein substrate, and a unique intramolecular channel acting to contain carbon monoxide within the protein and transfer it to the site needed for acetyl-CoA synthesis." @default.
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- W2094657311 date "2003-05-01" @default.
- W2094657311 modified "2023-09-23" @default.
- W2094657311 title "Acetate C–C bond formation and decomposition in the anaerobic world: the structure of a central enzyme and its key active-site metal cluster" @default.
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- W2094657311 doi "https://doi.org/10.1016/s0968-0004(03)00063-x" @default.
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