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Literature summary extracted from

  • Prince, R.C.; Hooper, A.B.
    Resolution of the hemes of hydroxylamine oxidoreductase by redox potentiometry and electron spin resonance spectroscopy (1987), Biochemistry, 26, 970-974.
No PubMed abstract available

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.6 Nitrosomonas europaea
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-
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Substrates and Products (Substrate)

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.2.6 heme resolution of the hemes by redox potentiometry and electron spin resonance spectroscopy Nitrosomonas europaea
1.7.2.6 heme multi-heme enzyme containing at least 5 thermodynamically distinct c-type hemes and the heme-like moiety P460 Nitrosomonas europaea