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Literature summary for 1.7.2.8 extracted from

  • Fernandez, M.L.; Estrin, D.A.; Bari, S.E.
    Theoretical insight into the hydroxylamine oxidoreductase mechanism (2008), J. Inorg. Biochem., 102, 1523-1530.
    View publication on PubMed
Search for more literature for 1.7.2.8

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ as Fe(II)NO in the c-type heme Nitrosomonas europaea

Organism

Organism UniProt Comment Textmining
Nitrosomonas europaea
-
-
-

Reaction

Reaction Comment Organism Reaction ID
hydroxylamine + NH3 + acceptor = N2 + H2O + reduced acceptor the meso tyrosyl residue enhances the binding of hydroxylamine, and increases the stability of a FeIIINO intermediate, while behaving indifferently in the FeIINO form, catalytic mechanism, modelling, overview Nitrosomonas europaea
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme catalyzes the conversion of hydroxylamine to nitrite, with a complicate arrangement of heme groups in three subunits Nitrosomonas europaea ?
-
 ?

Subunits

Subunits Comment Organism
trimer complicate arrangement of heme groups in three subunits. As a distinctive feature, the protein has a covalent linkage between a tyrosyl residue of one subunit and a meso carbon atom of the heme active site of another Nitrosomonas europaea

Cofactor

Cofactor Comment Organism Structure
cytochrome P460 cytochrome P460 heme, c-type heme, and planar heme, structure modelling, overview Nitrosomonas europaea