Literature DB >> 25307727

Selenate reductase activity in Escherichia coli requires Isc iron-sulfur cluster biosynthesis genes.

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.
© 2014 Federation of European Microbiological Societies. Published by John Wiley & Sons Ltd. All rights reserved.

Entities:  

Keywords:  Enterobacter; FNR; Salmonella; Suf; TAT; molybdoenzyme

Mesh:

Substances:

Year:  2014        PMID: 25307727     DOI: 10.1111/1574-6968.12623

Source DB:  PubMed          Journal:  FEMS Microbiol Lett        ISSN: 0378-1097            Impact factor:   2.742


  3 in total

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Review 2.  Selenium Metabolism and Selenoproteins in Prokaryotes: A Bioinformatics Perspective.

Authors:  Yan Zhang; Jiao Jin; Biyan Huang; Huimin Ying; Jie He; Liang Jiang
Journal:  Biomolecules       Date:  2022-06-29

3.  Analysis of Bioavailability and Induction of Glutathione Peroxidase by Dietary Nanoelemental, Organic and Inorganic Selenium.

Authors:  Mitchell T Ringuet; Billie Hunne; Markus Lenz; David M Bravo; John B Furness
Journal:  Nutrients       Date:  2021-03-25       Impact factor: 5.717

  3 in total

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