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Reduction of uranium by cytochrome c3 of Desulfovibrio vulgaris

Derek R. Lovley·P.K. Widman·J.C. Woodward·Elizabeth J.P. Phillips
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Abstract

The mechanism for U(VI) reduction by Desulfovibrio vulgaris (Hildenborough) was investigated. The H 2 -dependent U(VI) reductase activity in the soluble fraction of the cells was lost when the soluble fraction was passed over a cationic exchange column which extracted cytochrome c 3 . Addition of cytochrome c 3 back to the soluble fraction that had been passed over the cationic exchange column restored the U(VI)-reducing capacity. Reduced cytochrome c 3 was oxidized by U(VI), as was a c -type cytochrome(s) in whole-cell suspensions. When cytochrome c 3 was combined with hydrogenase, its physiological electron donor, U(VI) was reduced in the presence of H 2 . Hydrogenase alone could not reduce U(VI). Rapid U(VI) reduction was followed by a subsequent slow precipitation of the U(IV) mineral uraninite. Cytochrome c 3 reduced U(VI) in a uranium-contaminated surface water and groundwater. Cytochrome c 3 provides the first enzyme model for the reduction and biomineralization of uranium in sedimentary environments. Furthermore, the finding that cytochrome c 3 can catalyze the reductive precipitation of uranium may aid in the development of fixed-enzyme reactors and/or organisms with enhanced U(VI)-reducing capacity for the bioremediation of uranium- contaminated waters and waste streams.

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Derek R. Lovley, P.K. Widman, J.C. Woodward, Elizabeth J.P. Phillips. 1993. Reduction of uranium by cytochrome c3 of Desulfovibrio vulgaris. https://doi.org/10.1128/aem.59.11.3572-3576.1993

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