Sulfite reductase

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In enzymology, a sulfite reductase (EC 1.8.99.1) is an enzyme that catalyzes the chemical reaction

hydrogen sulfide + acceptor + 3 H₂O $\rightleftharpoons$ sulfite + reduced acceptor

The 3 substrates of this enzyme are hydrogen sulfide, acceptor, and H₂O, whereas its two products are sulfite and reduced acceptor.

This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with other acceptors. The systematic name of this enzyme class is hydrogen-sulfide:acceptor oxidoreductase. Other names in common use include assimilatory sulfite reductase, assimilatory-type sulfite reductase, and hydrogen-sulfide:(acceptor) oxidoreductase. This enzyme participates in selenoamino acid metabolism and sulfur assimilation. It employs one cofactor, iron.

[edit] References

IUBMB entry for 1.8.99.1
BRENDA references for 1.8.99.1 (Recommended.)
PubMed references for 1.8.99.1
PubMed Central references for 1.8.99.1
Google Scholar references for 1.8.99.1
Asada K (1967). "Purification and properties of a sulfite reductase from leaf tissue". J. Biol. Chem. 242: 3646–54. PMID 6038492.
Asada K, Tamura G, Bandurski RS (1969). "Methyl viologen-linked sulfite reductase from spinach leaves". J. Biol. Chem. 244: 4904–15. PMID 5824566.
Yoshimoto A, Nakamura T, Sato R (Tokyo). "Isolation from Aspergillus nidulans, of a protein catalyzing the reduction of sulfite by reduced viologen dyes". J. Biochem.: 756–66. PMID 5589532.