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- W2002076018 abstract "1. Hydrogenase (hydrogen: cytochrome c3 oxidoreductase) of high specific activity has been purified to near homogeneity as judged by disc electrophoresis and in the analytical ultracentrifuge, and found to contain 3.5 iron and 3.2 labile-sulfide atoms per molecule (of mol. wt. 60 000). 2. Hydrogenase was found to exist in a dimer form of mol. wt. 60 000 and a monomer form of 30 000. The dimer—monomer forms were concentration-dependent with the dimer form favored at high protein concentrations. 3. Light absorption and EPR studies definitely indicate a redox functional iron-sulfide unit at the active site. On reduction with H2, a g = 1.86 EPR absorption was observed. This is the Beinert “g = 1.9” type of EPR absorption observed in other iron-sulfide proteins such as plant and bacterial ferredoxins." @default.
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- W2002076018 date "1971-06-01" @default.
- W2002076018 modified "2023-09-26" @default.
- W2002076018 title "Evidence for the involvement of non-heme iron in the active site of hydrogenase from Desulfovibrio vulgaris" @default.
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- W2002076018 doi "https://doi.org/10.1016/0005-2728(71)90222-2" @default.
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