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Article

Molecular basis for enzymatic sulfite oxidation: how three conserved active site residues shape enzyme activity.

The Journal of biological chemistry - 23 Jan 2009

Bailey Susan, Rapson Trevor, Johnson-Winters Kayunta, Astashkin Andrei V, Enemark John H, Kappler Ulrike

Abstract excerpt

Sulfite dehydrogenases (SDHs) catalyze the oxidation and detoxification of sulfite to sulfate, a reaction critical to all forms of life. Sulfite-oxidizing enzymes contain three conserved active site amino acids (Arg-55, His-57, and Tyr-236) that are crucial for catalytic competency. Here we have studied the kinetic and structural effects of two novel and one previously reported substitution (R55M, H57A, Y236F) in...

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Identifiers

PMID: 19004819
DOI: 10.1074/jbc.M807718200
PMCID: PMC2629113

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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