Purification and properties of the hydrogenase of Desulfovibrio desulfuricans

Sadana, J. C. ; Jagannathan, V. (1956) Purification and properties of the hydrogenase of Desulfovibrio desulfuricans Biochimica et Biophysica Acta (BBA) - General Subjects, 19 . pp. 440-452. ISSN 0304-4165

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Related URL: http://dx.doi.org/10.1016/0006-3002(56)90467-X


Hydrogenase from Desulfovibrio desulfuricans has been purified about fifty-fold. At the highest level of purity 1 mg of protein N catalyses the oxidation of 2.6·106 μl of H2 per hour by methylene blue at 34°. Purified hydrogenase was found to be activated by FeCl2 or FeCl3, the increase in activity being the same with benzyl viologen or methylene blue as oxidant. A thermostable cytochrome-like component was obtained during the purification, which has no hydrogenase activity, but could be reduced by hydrogen and hydrogenase and reoxidised by O2, methylene blue or FMN. Methylene blue and benzyl viologen were reduced rapidly and at the same rate by hydrogen in the presence of purified hydrogenase; FMN, FAD and riboflavin were reduced at about one-hundredth of this rate, while DPN, TPN, sulfate and ferricyanide were not reduced. The optimum pH for methylene blue reduction was 8.4, cysteine or glutathione was essential for enzyme activity and serum albumin had a protective action at high enzyme dilutions. Hydrogenase was inhibited by p-chloromercuribenzoate and the inhibition was reversed by cysteine or glutathione. Cyanide and other metal-binding agents, hydroxylamine and nitrite were also inhibitory.

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