Hydrogenase from Acetobacterium woodii

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Abstract
Hydrogenase from fructose-grown cells of Acetobacterium woodii has been purified 70-fold to a specific activity of 3,500 μmol hydrogen oxidized per min per mg of protein measured at 35°C and pH 7.6 with methyl viologen as electron acceptor. At the same conditions with reduced methyl viologen as electron donor the enzyme catalyzes the evolvement of 440 μmol of H2 per min per mg of protein. The enzyme was found in the soluble portion of the cell, indicating that it is either not membrane-bound or is loosely associated with the membrane. The purified enzyme, which does not contain nickel, exhibits spectroscopic properties similar to the iron-sulfur hydrogenase of Clostridium pasteurianum. The enzyme is strongly inhibited by carbon monoxide, with 50% inhibition occurring at approximately 7 nM CO. Ferredoxin, flavodoxin, and carbon monoxide dehydrogenase are reduced in hydrogen-dependent reaction by the A. woodi hydrogenase.