Abstract
1. 1. Hydrogenase from D. desulfuricans has been purified about 1300-fold. At the highest level of purity, 1 mg of protein N catalyses the oxidation of 11·10 7 μl H 2 per hour by methylene blue at 38°. 2. 2. The purified enzyme was completely inactive without added iron ions. Requirement for molybdenum could not be demonstrated with either two- or one-electron acceptor dyes. 3. 3. The activity of purified hydrogenase was not affected by treatment of the enzyme with trypsin, chymotrypsin, carboxypeptidase, ribonuclease, snake venom phosphodiesterase, 5′-nucleotidase, and intestinal phosphatase. 4. 4. The activity of hydrogenase from D. desulfuricans as determined by the evolution of hydrogen from reduced methyl viologen was about 0.05 of that observed for the reduction of methylene blue. 5. 5. The purified enzyme was free from bacterial cytochrome. It was observed that bacterial cytochrome c 3 was required for the reduction of flavins but not for methylene blue.
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