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Literature summary for 1.8.1.2 extracted from

  • Siegel, L.M.; Rueger, D.C.; Barber, M.J.; Krueger, R.J.; Orme-Johnson, N.R.; Orme-Johnson, W.H.
    Escherichia coli sulfite reductase hemoprotein subunit. Prosthetic groups, catalytic parameters, and ligand complexes (1982), J. Biol. Chem., 257, 6343-6350.
    View publication on PubMed
Search for more literature for 1.8.1.2

Inhibitors

Inhibitors Comment Organism Structure
CN-
-
 Escherichia coli
CO
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.012 0.017 sulfite
-
 Escherichia coli
0.8 1.5 nitrite
-
 Escherichia coli
4.5 10.5 hydroxylamine
-
 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Iron-sulfur cluster hemoprotein subunit contains one siroheme and one Fe4S4 center per polypeptide, heme is in high spin Fe3+ state Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hydroxylamine + NADPH
-
 Escherichia coli ammonia + NADP+
-
 ?
additional information reduction of sulfite, nitrite, and hydroxylamine by NADPH requires catalytic activities of both subunits, reduction of sulfite, nitrite, and hydroxylamine by methyl viologen requires hemoprotein subunit Escherichia coli ?
-
 ?
nitrite + NADPH NADPH can be replaced by reduced methyl viologen, the latter reaction is catalyzed by hemoprotein subunit alone Escherichia coli ammonia + NADP+
-
 ?
sulfite + NADPH NADPH can be replaced by reduced methyl viologen Escherichia coli sulfide + NADP+ + H2O
-
 ?

Cofactor

Cofactor Comment Organism Structure
heme hemoprotein subunit contains one siroheme and one Fe4S4 center per polypeptide Escherichia coli