Journal
FEBS LETTERS
Volume 581, Issue 29, Pages 5605-5610Publisher
WILEY
DOI: 10.1016/j.febslet.2007.11.008
Keywords
oxidative stress; superoxide reductase; anaerobic bacteria; Clostridium
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Desulfoferrodoxin (cac2450) of Clostridium acetobutylicum was purified after overexpression in E. coli. In an in vitro assay the enzyme exhibited superoxide reductase activity with rubredoxin (cac2778) of C. acetobutylicum as the proximal electron donor. Rubredoxin was reduced by ferredoxin: NADP+ reductase from spinach and NADPH. The superoxide anions, generated from dissolved oxygen using Xanthine and Xanthine oxidase, were reduced to hydrogen peroxide. Thus, we assume that desulfoferrodoxin is the key factor in the superoxide reductase dependent part of an alternative pathway for detoxification of reactive oxygen species in this obligate anaerobic bacterium. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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