Literature summary for 1.7.2.6 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.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
to 2.1 A resolution. Heme P460 contains two covalent cross-links between the porphyrin and a Tyr residue. When purified from source, an unknown physiological HAO binding partner NE1300 is present within the crystal. Protein NE1300 may play a structural role in the ternary complex with cytochrome c554, the physiological electron acceptor of the enzyme	Nitrosomonas europaea

Organism

Organism	UniProt	Comment	Textmining
Nitrosomonas europaea	Q50925	-	-
Nitrosomonas europaea ATCC 19718	Q50925	-	-

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Release 2023.1 (January 2023)