Reduction of uranium by cytochrome c3 of Desulfovibrio vulgaris

Applied and Environmental Microbiology
By: , and 


  • The Publications Warehouse does not have links to digital versions of this publication at this time
  • Download citation as: RIS | Dublin Core


The mechanism for U(VI) reduction by Desulfovibrio vulgaris (Hildenborough) was investigated. The H2-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 c3. Addition of cytochrome c3 back to the soluble fraction that had been passed over the cationic exchange column restored the U(VI)-reducing capacity. Reduced cytochrome c3 was oxidized by U(VI), as was a c-type cytochrome(s) in whole-cell suspensions. When cytochrome c3 was combined with hydrogenase, its physiological electron donor, U(VI) was reduced in the presence of H2. 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 c3 reduced U(VI) in a uranium-contaminated surface water and groundwater. Cytochrome c3 provides the first enzyme model for the reduction and biomineralization of uranium in sedimentary environments. Furthermore, the finding that cytochrome c3 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.

Additional publication details

Publication type Article
Publication Subtype Journal Article
Title Reduction of uranium by cytochrome c3 of Desulfovibrio vulgaris
Series title Applied and Environmental Microbiology
Volume 59
Issue 11
Year Published 1993
Language English
Larger Work Type Article
Larger Work Subtype Journal Article
Larger Work Title Applied and Environmental Microbiology
First page 3572
Last page 3576