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Article

Kinetic and structural evidence for the importance of Tyr236 for the integrity of the Mo active site in a bacterial sulfite dehydrogenase.

Biochemistry - 15 Aug 2006

Kappler Ulrike, Bailey Susan, Feng Changjian, Honeychurch Michael J, Hanson Graeme R, Bernhardt Paul V, Tollin Gordon, Enemark John H

Abstract excerpt

The sulfite dehydrogenase from Starkeya novella is the only known sulfite-oxidizing enzyme that forms a permanent heterodimeric complex between a molybdenum and a heme c-containing subunit and can be crystallized in an electron transfer competent conformation. Tyr236 is a highly conserved active site residue in sulfite oxidoreductases and has been shown to interact with a nearby arginine and a molybdenum-oxo...

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PMID: 16893171
DOI: 10.1021/bi060058b

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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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Kinetic and structural evidence for the importance of Tyr236 for the integrity of the Mo active site in a bacterial sulfite dehydrogenase.PMID 16893171Read ↗

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