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Article

Coordination chemistry at the molybdenum site of sulfite oxidase: redox-induced structural changes in the cysteine 207 to serine mutant.

Inorganic chemistry - 27 Dec 2004

George Graham N, Garrett Robert M, Prince Roger C, Rajagopalan K V

Abstract excerpt

The redox chemistry of the molybdenum site of the C207S mutant of recombinant human sulfite oxidase has been studied via potentiometric titrations employing both electron paramagnetic resonance (EPR) spectroscopy and X-ray absorption spectroscopy (XAS) as probes of the active site structure. In earlier EXAFS studies, oxidized Cys207Ser enzyme has been shown to possess a novel tri-oxo active site, in which Ser207...

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Identifiers

PMID: 15606194
DOI: 10.1021/ic0489847

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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