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Article

Dioxygen activation at non-heme diiron centers: oxidation of a proximal residue in the I100W variant of toluene/o-xylene monooxygenase hydroxylase.

Biochemistry - 25 Dec 2007

Murray Leslie J, García-Serres Ricardo, McCormick Michael S, Davydov Roman, Naik Sunil G, Kim Sun-Hee, Hoffman Brian M, Huynh Boi Hanh, Lippard Stephen J

Abstract excerpt

At its carboxylate-bridged diiron active site, the hydroxylase component of toluene/o-xylene monooxygenase activates dioxygen for subsequent arene hydroxylation. In an I100W variant of this enzyme, we characterized the formation and decay of two species formed by addition of dioxygen to the reduced, diiron(II) state by rapid-freeze quench (RFQ) EPR, Mössbauer, and ENDOR spectroscopy. The dependence of the...

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Identifiers

PMID: 18044971
DOI: 10.1021/bi7017128
PMCID: PMC2494530

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