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Article

Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer.

Biochemistry - 11 Dec 2012

Smith Kyle W, Stroupe M Elizabeth

Abstract excerpt

Sulfite reductase catalyzes the six-electron reduction of sulfite to sulfide. The active site, found in the hemoprotein subunit (SiRHP), sits on the distal face of a negatively charged porphyrinoid called siroheme whose central iron atom is coupled to a proximal Fe(4)S(4) cluster. Four positively charged amino acids are positioned around the active site cavity. Together, these two arginines (R83 and R153) and two...

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PMID: 23153334
DOI: 10.1021/bi300947a

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

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