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The superoxide radical O(2)(-.) is a toxic by-product of oxygen metabolism.Two O(2)(-.) detoxifying enzymes have been described so far, superoxidedismutase and superoxide reductase (SOR), both forming H2O2 as a reactionproduct. Recently, the SOR active site, a ferrous iron in a [Fe(2+) (N-His)(4)(S-Cys)] pentacoordination, was shown to have the ability to form a complexwith the organometallic compound ferrocyanide. Here, we have investigated indetail the reactivity of the SOR-ferrocyanide complex with O(2)(-.) by pulseand gamma-ray radiolysis, infrared, and UV-visible spectroscopies. The complexreacts very efficiently with O(2)(-.). However, the presence of theferrocyanide adduct markedly modifies the reaction mechanism of SOR, with theformation of transient intermediates different from those observed for SORalone. A one-electron redox chemistry appears to be carried out by theferrocyanide moiety of the complex, whereas the SOR iron site remains in thereduced state. Surprisingly, the toxic H2O2 species is no longer the reactionproduct. Accordingly, in vivo experiments showed that formation of theSOR-ferrocyanide complex increased the antioxidant capabilities of SORexpressed in an Escherichia coli sodA sodB recA mutant strain. Altogether,these data describe an unprecedented O(2)(-.) detoxification activity,catalyzed by the SOR-ferrocyanide complex, which does not conduct to theproduction of the toxic H2O2 species.

Detoxification of superoxide without production of H2O2: antioxidant activity of superoxide reductase complexed with ferrocyanide