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Updated: Jul 10, 2026

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
Published on: February 24, 2018
Desulfoferrodoxin of Clostridium acetobutylicum functions as a superoxide reductase
Oliver Riebe1, Ralf-Jörg Fischer, Hubert Bahl
1University of Rostock, Institute of Biological Sciences, Division of Microbiology, Albert-Einstein-Strasse 3, D-18051, Rostock, Germany.
Abstract:
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.
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