Desulfoferrodoxin of Clostridium acetobutylicum functions as a superoxide reductase.
FEBS Lett
; 581(29): 5605-10, 2007 Dec 11.
Article
em En
| MEDLINE
| ID: mdl-18005665
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 ferredoxinNADP(+) 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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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oxirredutases
/
Proteínas de Bactérias
/
Clostridium acetobutylicum
/
Ferredoxinas
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2007
Tipo de documento:
Article
País de afiliação:
Alemanha