Chromium(VI) reductase activity is associated with the cytoplasmic membrane of anaerobically grown Shewanella putrefaciens MR-1. J Appl Microbiol 2000 Jan;88(1):98-106
Date
03/29/2000Pubmed ID
10735248DOI
10.1046/j.1365-2672.2000.00910.xScopus ID
2-s2.0-0034091960 (requires institutional sign-in at Scopus site) 237 CitationsAbstract
Shewanella putrefaciens MR-1 can reduce a diverse array of compounds under anaerobic conditions, including manganese and iron oxides, fumarate, nitrate, and many other compounds. These reductive processes are apparently linked to a complex electron transport system. Chromium (Cr) is a toxic and mutagenic metal and bacteria could potentially be utilized to immobilize Cr by reducing the soluble and bioavailable state, Cr(VI), to the insoluble and less bioavailable state, Cr(III). Formate-dependent Cr(VI) reductase activity was detected in anaerobically grown cells of S. putrefaciens MR-1, with highest specific activity in the cytoplasmic membrane. Both formate and NADH served as electron donors for Cr(VI) reductase, whereas L-lactate or NADPH did not support any activity. The addition of 10 micromol l(-1) FMN markedly stimulated formate-dependent Cr(VI) reductase, and the activity was almost completely inhibited by diphenyliodonium chloride, an inhibitor of flavoproteins. Cr(VI) reductase activity was also inhibited by p-chloromercuriphenylsulphonate, azide, 2-heptyl-4-hydroxyquinolone-N-oxide, and antimycin A, suggesting involvement of a multi-component electron transport chain which could include cytochromes and quinones. Cr(V) was detected by electron paramagnetic resonance (EPR) spectroscopy, suggesting a one-electron reduction as the first step.
Author List
Myers CR, Carstens BP, Antholine WE, Myers JMMESH terms used to index this publication - Major topics in bold
AnaerobiosisElectron Spin Resonance Spectroscopy
Electron Transport
Enzyme Inhibitors
Flavin Mononucleotide
Formates
Intracellular Membranes
NAD
Oxidoreductases
Shewanella putrefaciens
