Selenite reduction in clostridium pasteurianum
Date
1990
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Abstract
Selenite reduction in Clostridium pasteurianum was determined to be due to the constitutive activity of the hydrogenase I enzyme. 115 fold purification of this enzyme was achieved, with strong activity in both Tris and phosphate buffers being seen for selenite reduction. The Vmax for the reduction of selenite was determined to be 158 µmoles hydrogen uptake/min/mg protein, with the Km being 0.2 mM for selenite. The theoretical stoichiometry for the reduction of selenite to elemental selenium, 2 H2 consumed to 1 Se0 produced, was found be close to the experimentally determined value of 2.3:1, and no intermediates in the reduction process were found. The reductase activity was quite specific for selenite and tellurite substrates, and could be efficiently linked by a variety of electron carriers, including the presumed physiological carrier ferredoxin.
Description
Bibliography: p. 79-93.
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Citation
Yanke, L. J. (1990). Selenite reduction in clostridium pasteurianum (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/17105