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Desulfoferrodoxin of Clostridium acetobutylicum functions as a superoxide reductase
Author(s) -
Riebe Oliver,
Fischer Ralf-Jörg,
Bahl Hubert
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.11.008
Subject(s) - clostridium acetobutylicum , superoxide , chemistry , biochemistry , reductase , xanthine oxidase , reactive oxygen species , superoxide dismutase , ferredoxin , desulfovibrio , enzyme , butanol , organic chemistry , ethanol , sulfate
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.