Abstract
Three soluble molecular forms of hydrogenase have been isolated from various Desulfovibrio species (1). Well characterized hydrogenases representative of each of these forms are: the periplasmic hydrogenase from D. vulgaris (2) which contains exclusively non-heme iron (Fe hydrogenase); the periplasmic nickel non-heme iron selenium hydrogenase ((Ni Fe Se) hydrogenase) from D. gigas (3, 4); and the nickel iron selenium hydrogenase (Ni Fe Se) hydrogenase) from D. desulfuricans (5). These hydrogenases differ in their metal centre composition, mechanistic properties (6), sensitivity to inhibitors (7), amino acid sequences (1) and immunological properties (8). All these hydrogenases have in common the capability to reduce directly the tetrahemic low potential cytochrome c3 under hydrogen atmosphere (9, 10).
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