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Literature summary for 1.8.1.2 extracted from

  • Cepeda, M.R.; McGarry, L.; Pennington, J.M.; Krzystek, J.; Stroupe, M.E.
    The role of extended Fe4S4 cluster ligands in mediating sulfite reductase hemoprotein activity (2018), Biochim. Biophys. Acta Proteins Proteom., 1866, 933-940 .
    View publication on PubMed
Search for more literature for 1.8.1.2

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Escherichia coli

Protein Variants

Protein Variants Comment Organism
F437A the variant is more reactive when reduced chemically, likely because the chemical reductant has superior access to the active site, the variant is also more active as part of the dodecamer Escherichia coli
M444A the variant is more reactive when reduced chemically, likely because the chemical reductant has superior access to the active site, the variant is not more active as part of the dodecamer Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sulfite + 3 NADPH + 3 H+ Escherichia coli
-
 hydrogen sulfide + 3 NADP+ + 3 H2O
-
 ?
sulfite + 3 NADPH + 3 H+ Escherichia coli K12
-
 hydrogen sulfide + 3 NADP+ + 3 H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P17846 sulfite reductase [NADPH] hemoprotein beta-component
-
Escherichia coli K12 P17846 sulfite reductase [NADPH] hemoprotein beta-component
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sulfite + 3 NADPH + 3 H+
-
 Escherichia coli hydrogen sulfide + 3 NADP+ + 3 H2O
-
 ?
sulfite + 3 NADPH + 3 H+
-
 Escherichia coli K12 hydrogen sulfide + 3 NADP+ + 3 H2O
-
 ?

Synonyms

Synonyms Comment Organism
NADPH-dependent sulfite reductase
-
 Escherichia coli
SiR/SiRHP
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
siroheme siroheme-containing subunit of the multimeric hemoflavoprotein NADPH-dependent sulfite reductase. Siroheme is an iron-containing isobacteriochlorin, that does not work alone but is covalently coupled to a Fe4S4 cluster through one of the cluster's ligands Escherichia coli