Literature summary extracted from

Terry, K.R.; Hooper, A.B.
Hydroxylamine oxidoreductase: a 20-heme, 200 000 molecular weight cytochrome c with unusual denaturation properties which forms a 63 000 molecular weight monomer after heme removal (1981), Biochemistry, 20, 7026-7032.

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1.7.2.6	11000	-	3 * 63000 + 3 * 11000, (alpha,beta)3 subunit structure, SDS-PAGE, 200000 MW enzyme forms a 63000 MW monomer after heme removal, hydroxylamine oxidoreductase probably consists of 3 molecules of monoheme c-type cytochrome with a MW of 11000 and 3 tightly complexed molecules of a catalytically active MW 63000 protein containing 6 c-type hemes and one P-460 heme, SDS-PAGE	Nitrosomonas europaea
1.7.2.6	63000	-	3 * 63000 + 3 * 11000, (alpha,beta)3 subunit structure, SDS-PAGE, 200000 MW enzyme forms a 63000 MW monomer after heme removal, hydroxylamine oxidoreductase probably consists of 3 molecules of monoheme c-type cytochrome with a MW of 11000 and 3 tightly complexed molecules of a catalytically active MW 63000 protein containing 6 c-type hemes and one P-460 heme, SDS-PAGE	Nitrosomonas europaea
1.7.2.6	180000	200000	SDS-PAGE	Nitrosomonas europaea

Organism

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

Subunits

EC Number	Subunits	Comment	Organism
1.7.2.6	hexamer	3 * 63000 + 3 * 11000, (alpha,beta)3 subunit structure, SDS-PAGE, 200000 MW enzyme forms a 63000 MW monomer after heme removal, hydroxylamine oxidoreductase probably consists of 3 molecules of monoheme c-type cytochrome with a MW of 11000 and 3 tightly complexed molecules of a catalytically active MW 63000 protein containing 6 c-type hemes and one P-460 heme, SDS-PAGE	Nitrosomonas europaea

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.7.2.6	heme	-	Nitrosomonas europaea

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Release 2023.1 (January 2023)