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J Bacteriol. 1971 January; 105(1): 249-258
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Purification and Properties of a Hydrogenase from Desulfovibrio vulgaris¹

^a Department of Microbiology, University of Illinois, Urbana, Illinois 61801

ABSTRACT

The soluble hydrogenase of Desulfovibrio vulgaris was purified and some of its properties are described. The molecular weight was determined for the enzyme by sedimentation equilibrium (45,400) and amino acid analysis (44,800). The hydrogenase appears to be a loosely coiled molecule or to have a high axial ratio, which is reflected in an unusually low sedimentation coefficient (2.58S) and a low diffusion coefficient (D 5.85). The molecular weight of the hydrogenase (41,000), as calculated by the Svedberg equation, was in general agreement with the sedimentation equilibrium molecular weight. Amino acid analysis revealed the presence of six halfcystine residues per mole of enzyme and a total of 417 amino acid residues. The specificity of the hydrogenase and its capacity to reduce certain low potential dyes and cytochrome c₃ was studied. Metal analysis of the hydrogenase indicated the presence of 1 mole of ferrous iron per mole of enzyme.

¹ Taken in part from the dissertation of R. H. Haschke presented to the Graduate Faculty of the University of Illinois, Urbana, in partial fulfillment of requirements for the Ph.D. degree (1969).