A Functional Model for the Cysteinate-Ligated Non-Heme Iron Enzyme Superoxide Reductase (SOR)

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A functional model for the cysteinate-ligated non-heme iron enzyme superoxide reductase (SOR).

Superoxide reductases (SORs) are cysteine-ligated, non-heme iron enzymes that reduce toxic superoxide radicals (O2-). The functional role of the trans cysteinate, as well as the mechanism by which SOR reduces O2-, is unknown. Herein is described a rare example of a functional metalloenzyme analogue, which catalytically reduces superoxide in a proton-dependent mechanism, via a trans thiolate-lig...

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Synthetic Models for the Cysteinate-Ligated Non-Heme Iron Enzyme Superoxide Reductase: Observation and Structural Characterization by XAS of an Fe-OOH Intermediate

Superoxide reductases (SORs) belong to a new class of metalloenzymes that degrade superoxide by reducing it to hydrogen peroxide. These enzymes contain a catalytic iron site that cycles between the FeII and FeIII states during catalysis. A key step in the reduction of superoxide has been suggested to involve HO2 binding to FeII, followed by innersphere electron transfer to afford an FeIII-OO(H)...

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Synthetic models for the cysteinate-ligated non-heme iron enzyme superoxide reductase: observation and structural characterization by XAS of an Fe(III)-OOH intermediate.

Superoxide reductases (SORs) belong to a new class of metalloenzymes that degrade superoxide by reducing it to hydrogen peroxide. These enzymes contain a catalytic iron site that cycles between the Fe(II) and Fe(III) states during catalysis. A key step in the reduction of superoxide has been suggested to involve HO(2) binding to Fe(II), followed by innersphere electron transfer to afford an Fe(...

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Non-heme iron hydroperoxo species in superoxide reductase as a catalyst for oxidation reactions.

The non-heme high-spin ferric iron hydroperoxo species formed in superoxide reductase catalyzes oxidative aldehyde deformylation through its nucleophilic character. This species also acts as an electrophile to catalyze oxygen atom transfer in sulfoxidation reactions, highlighting the oxidation potential of non-heme iron hydroperoxo species.

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The active site of superoxide reductase SOR consists of an Fe2+ center in an unusual [His4 Cys1] square-pyramidal geometry. It specifically reduces superoxide to produce H2O2. Here, we have reacted the SOR from Desulfoarculus baarsii directly with H2O2. We have found that its active site can transiently stabilize an Fe3+-peroxo species that we have spectroscopically characterized by resonance R...

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ژورنال

عنوان ژورنال: Journal of the American Chemical Society

سال: 2006

ISSN: 0002-7863,1520-5126

DOI: 10.1021/ja064870d