1. Intermolecular electron transfer in two-iron superoxide reductase: a putative role for the desulforedoxin center as an electron donor to the iron active site.
- Author
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Bonnot, Florence, Duval, Simon, Lombard, Murielle, Valton, Julien, Houée-Levin, Chantal, and Nivière, Vincent
- Subjects
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OXIDATION-reduction reaction , *IRON compounds , *NAD(P)H dehydrogenases , *ELECTRON donor-acceptor complexes , *HYDROGEN peroxide , *COORDINATION compounds , *ENZYME kinetics - Abstract
Superoxide reductase (SOR) is a superoxide detoxification system present in some microorganisms. Its active site consists of an unusual mononuclear iron center with an FeN4S1 coordination which catalyzes the one-electron reduction of superoxide to form hydrogen peroxide. Different classes of SORs have been described depending on the presence of an additional rubredoxin-like, desulforedoxin iron center, whose function has remained unknown until now. In this work, we investigated the mechanism of the reduction of the SOR iron active site using the NADPH:flavodoxin oxidoreductase from Escherichia coli, which was previously shown to efficiently transfer electrons to the Desulfoarculus baarsii SOR. When present, the additional rubredoxin-like iron center could function as an electronic relay between cellular reductases and the iron active site for superoxide reduction. This electron transfer was mainly intermolecular, between the rubredoxin-like iron center of one SOR and the iron active site of another SOR. These data provide the first experimental evidence for a possible role of the rubredoxin-like iron center in the superoxide detoxifying activity of SOR. [ABSTRACT FROM AUTHOR]
- Published
- 2011
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