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• W4237402557 abstract "The electrode reaction of the soluble domain of membrane-bound hydrogenase from Desulfovibrio vulgaris, Miyazaki F, was studied at mercury and six other solid electrodes. A cathodic wave at −0.30 V (vs. NHE) at pH 7.0 observed for hydrogenase adsorbed on a mercury electrode is attributed to the reduction of the active center of hydrogenase, the iron-sulfur cluster. This reduction process involves proton transfer. Once reduced, the hydrogenase loses its reoxidation activity at the mercury electrode. Hydrogenase adsorbed on a mercury electrode catalyzes the hydrogen production reaction, whose onset potential at pH 7.0 is 120 mV more positive than the reversible hydrogen electrode potential. The catalytic activity disappears when hydrogenase is thiocarboxymethylated, while the reduction activity of the active center is retained." @default.
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• W4237402557 date "1992-08-01" @default.
• W4237402557 modified "2023-10-18" @default.
• W4237402557 title "Electrode reaction of the soluble domain of the membrane-bound hydrogenase from Desulfovibrio vulgaris, strain Miyazaki F" @default.
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• W4237402557 doi "https://doi.org/10.1016/0302-4598(92)80012-6" @default.
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