Literature summary extracted from

Hooper, A.B.; Tran, M.; Balny, C.
Kinetics of reduction by substrate or dithionite and heme-heme electron transfer in the multiheme hydroxylamine oxidoreductase (1984), Eur. J. Biochem., 141, 565-571.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
1.7.2.6	CO	-	Nitrosomonas europaea

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.7.2.6	Nitrosomonas europaea	-	-	-

Turnover Number [1/s]

EC Number	Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
1.7.2.6	additional information	-	additional information	overview: effect of pH on rate of reduction of heme c553 of the enzyme by NH2OH, rate constant for reduction of hemes of the enzyme by dithionite at 2°C and 19°C and by NH2OH or NH2NH2 at 2°C	Nitrosomonas europaea

pH Optimum

EC Number	pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
1.7.2.6	10.5	-	rate of reduction of hemes c 553 of the enzyme increases with pH	Nitrosomonas europaea

pH Stability

EC Number	pH Stability	pH Stability Maximum	Comment	Organism
1.7.2.6	10.5	-	enzyme is permanently inactivated above pH 10.5	Nitrosomonas europaea

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.7.2.6	heme	contains hemes c-553, c-559 and P-460 in the ratio 5:2:1, P-460 is the site of electron entry	Nitrosomonas europaea

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)