ExplorEnz: EC 1.8.1.2

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1.8.1.2

Accepted name:

assimilatory sulfite reductase (NADPH)

Reaction:

hydrogen sulfide + 3 NADP⁺ + 3 H₂O = sulfite + 3 NADPH + 3 H⁺

Other name(s):

sulfite reductase (NADPH); sulfite (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH-sulfite reductase; NADPH-dependent sulfite reductase; H₂S-NADP oxidoreductase; sulfite reductase (NADPH₂); MET5 (gene name); MET10 (gene name); cysI (gene name); cysJ (gene name)

Systematic name:

hydrogen-sulfide:NADP⁺ oxidoreductase

Comments:

Contains siroheme, [4Fe-4S] cluster, FAD and FMN. The enzyme, which catalyses the six-electron reduction of sulfite to sulfide, is involved in sulfate assimilation in bacteria and yeast. Different from EC 1.8.99.5, dissimilatory sulfite reductase, which is involved in prokaryotic sulfur-based energy metabolism. cf. EC 1.8.7.1, assimilatory sulfite reductase (ferredoxin).

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9029-35-0

References:

1.	Hilz, H., Kittler, M. and Knape, G. Die Reduktion von Sulfate in der Hefe. Biochem. Z. 332 (1959) 151–166. [PMID: 14401842]
2.	Yoshimoto, A. and Sato, R. Studies on yeast sulfite reductase. I. Purification and characterization. Biochim. Biophys. Acta 153 (1968) 555–575. [DOI] [PMID: 4384979]
3.	Siegel, L.M., Murphy, M.J. and Kamin, H. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. I. The Escherichia coli hemoflavoprotein: molecular parameters and prosthetic groups. J. Biol. Chem. 248 (1973) 251–264. [PMID: 4144254]
4.	Kobayashi, K. and Yoshimoto, A. Studies on yeast sulfite reductase. IV. Structure and steady-state kinetics. Biochim. Biophys. Acta 705 (1982) 348–356. [DOI] [PMID: 6751400]
5.	Siegel, L.M., Rueger, D.C., Barber, M.J., Krueger, R.J., Orme-Johnson, N.R. and Orme-Johnson, W.H. Escherichia coli sulfite reductase hemoprotein subunit. Prosthetic groups, catalytic parameters, and ligand complexes. J. Biol. Chem. 257 (1982) 6343–6350. [PMID: 6281269]
6.	Coves, J., Zeghouf, M., Macherel, D., Guigliarelli, B., Asso, M. and Fontecave, M. Flavin mononucleotide-binding domain of the flavoprotein component of the sulfite reductase from Escherichia coli. Biochemistry 36 (1997) 5921–5928. [DOI] [PMID: 9153434]
7.	Crane, B.R., Siegel, L.M. and Getzoff, E.D. Structures of the siroheme- and Fe₄S₄-containing active center of sulfite reductase in different states of oxidation: heme activation via reduction-gated exogenous ligand exchange. Biochemistry 36 (1997) 12101–12119. [DOI] [PMID: 9315848]

[EC 1.8.1.2 created 1961, modified 2015]