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Lookup NU author(s): Dr Carys WattsORCiD, James Leaver, Dr Clive Butler
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Enterobacter cloacae SLD1a-1 is capable of reducing selenium oxyanions to elemental selenium under both aerobic and anaerobic conditions. In this study the enzyme that catalyses the initial reduction of selenate (SeO 42-) to selenite (SeO32-) has been localised to isolated cytoplasmic membrane fractions. Experiments with intact cells have shown that the putative selenate reductase can accept electrons more readily from membrane-impermeable methyl viologen than membrane-permeable benzyl viologen, suggesting that the location of the catalytic site is towards the periplasmic side of the cytoplasmic membrane. Enzyme activity was enhanced by growing cells in the presence of 1 mM sodium molybdate and significantly reduced in cells grown in the presence of 1 mM sodium tungstate. Non-denaturing polyacrylamide gel electrophoresis (PAGE) gels stained for selenate and nitrate reductase activity have revealed that two distinct membrane-bound enzymes catalyse the reduction of selenate and nitrate. The role of this membrane-bound molybdenum-dependent reductase in relation to selenate detoxification and energy conservation is discussed. © 2003 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
Author(s): Watts CA, Ridley H, Condie KL, Leaver JT, Richardson DJ, Butler CS
Publication type: Article
Publication status: Published
Journal: FEMS Microbiology Letters
Year: 2003
Volume: 228
Issue: 2
Pages: 273-279
ISSN (print): 0378-1097
ISSN (electronic): 1574-6968
Publisher: Wiley-Blackwell Publishing
URL: http://dx.doi.org/10.1016/S0378-1097(03)00782-1
DOI: 10.1016/S0378-1097(03)00782-1
PubMed id: 14638434
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