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Literature summary extracted from

  • Cedervall, P.; Hooper, A.B.; Wilmot, C.M.
    Structural studies of hydroxylamine oxidoreductase reveal a unique heme cofactor and a previously unidentified interaction partner (2013), Biochemistry, 52, 6211-6218 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.7.3.6 purified native enzyme, mixing of 0.002 ml of protein in 20 mM Tris-HCl, pH 8.1, with 0.002 ml of crystallization solution containing 0.1 M potassium nitrate, 0.1 M MES-Na buffer, pH 7.5, and 46% v/v PEG 400, X-ray diffraction structure determination and analysis at 2.1 A resolution, modelling Nitrosomonas europaea

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.7.3.6 periplasm
-
Nitrosomonas europaea
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.3.6 hydroxylamine + 2 ferricytochrome c Nitrosomonas europaea
-
nitroxyl + 2 ferrocytochrome c + 2 H+
-
?
1.7.3.6 nitroxyl + 2 ferrocytochrome c + O2 + H+ Nitrosomonas europaea
-
nitrite + 2 ferricytochrome c + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.7.3.6 Nitrosomonas europaea Q82V11
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.3.6 native enzyme by ammonium sulfate fractionation, gel filtration, ultracentrifugation, again gel filtration, followed by anion exchange chromatography Nitrosomonas europaea

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.3.6 hydroxylamine + 2 ferricytochrome c
-
Nitrosomonas europaea nitroxyl + 2 ferrocytochrome c + 2 H+
-
?
1.7.3.6 nitroxyl + 2 ferrocytochrome c + O2 + H+
-
Nitrosomonas europaea nitrite + 2 ferricytochrome c + H2O
-
?

Subunits

EC Number Subunits Comment Organism
1.7.3.6 homotrimer 3 * 67000, SDS-PAGE Nitrosomonas europaea

Synonyms

EC Number Synonyms Comment Organism
1.7.3.6 HAO
-
Nitrosomonas europaea
1.7.3.6 hydroxylamine oxidoreductase
-
Nitrosomonas europaea
1.7.3.6 protein NE1300
-
Nitrosomonas europaea

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.3.6 cytochrome c554
-
Nitrosomonas europaea
1.7.3.6 cytochrome P-460 one heme in each HAO monomer is a highly unusual heme P460 that is the site of catalysis. Heme P460 contains two covalent cross-links between the porphyrin and a Tyr residue, structure analysis, overview Nitrosomonas europaea
1.7.3.6 heme hydroxylamine oxidoreductase is a 24-heme homotrimeric enzyme Nitrosomonas europaea

General Information

EC Number General Information Comment Organism
1.7.3.6 additional information one heme in each HAO monomer is a highly unusual heme P460 that is the site of catalysis, Enzyme structure analysis and molecular docking, modelling Nitrosomonas europaea
1.7.3.6 physiological function enzyme HAO catalyzes the conversion of hydroxylamine to nitrite in nitrifying bacteria, that is key reaction in the nitrogen cycle. The enzyme HAO, protein NE1300, may play a structural role in the ternary complex with cytochrome c554, the physiological electron acceptor of HAO. Two of HAO's product electrons are subsequently transferred back to ammonia monooxygenase as substrate electrons, and the other two electrons contribute to the electrochemical gradient through a terminal oxidase in the cytoplasmic membrane Nitrosomonas europaea