| Literature DB >> 25307727 |
Nathan Yee1, Jessica Choi, Abigail W Porter, Sean Carey, Ines Rauschenbach, Arye Harel.
Abstract
The selenate reductase in Escherichia coli is a multi-subunit enzyme predicted to bind Fe-S clusters. In this study, we examined the iron-sulfur cluster biosynthesis genes that are required for selenate reductase activity. Mutants devoid of either the iscU or hscB gene in the Isc iron-sulfur cluster biosynthesis pathway lost the ability to reduce selenate. Genetic complementation by the wild-type sequences restored selenate reductase activity. The results indicate the Isc biosynthetic system plays a key role in selenate reductase Fe-S cofactor assembly and is essential for enzyme activity.Entities:
Keywords: Enterobacter; FNR; Salmonella; Suf; TAT; molybdoenzyme
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Year: 2014 PMID: 25307727 DOI: 10.1111/1574-6968.12623
Source DB: PubMed Journal: FEMS Microbiol Lett ISSN: 0378-1097 Impact factor: 2.742