Affiliation:
1. 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 (2.58
S
) 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
c
3
was studied. Metal analysis of the hydrogenase indicated the presence of 1 mole of ferrous iron per mole of enzyme.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
53 articles.
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1. Biological Iron–Sulfur Clusters with Catalytic Activity;Bioinorganic Catalysis;1999-02-02
2. Nickel hydrogenases: in search of the active site;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1994-12
3. Electrochemical investigation of intermolecular electron-transfer between two physiological partners;Journal of Electroanalytical Chemistry and Interfacial Electrochemistry;1991-09
4. The structure and mechanism of iron-hydrogenases;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1990-11
5. Hydrogenase Genes in Desulfovibrio;Microbiology and Biochemistry of Strict Anaerobes Involved in Interspecies Hydrogen Transfer;1990