Literature summary extracted from

Zhao, B.; Guengerich, F.P.; Voehler, M.; Waterman, M.R.
Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer (2005), J. Biol. Chem., 280, 42188-42197.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.14.19.69	complex of ferric CYP158A2 with substrate analogue 2-hydroxy-1,4-naphthoquinone, 2.15 A resolution, and the flaviolin ferrous dioxygen-bound CYP158A2 complex, to 1.8 A resolution. In the ferrous dioxygen-bound flaviolin complex, the three water molecules in the ferric flaviolin complex still occupy the same positions and form hydrogen bonds to the distal dioxygen atom. A continuous hydrogen-bonded water network connecting the active site to the protein surface is proposed to participate in the proton-delivery cascade, leading to dioxygen bond scission	Streptomyces coelicolor

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.19.69	Streptomyces coelicolor	-	isoform CYP158A2	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.14.19.69	2-hydroxy-1,4-naphthoquinone + reduced ferredoxin [iron-sulfur] cluster + H+ + O2	-	Streptomyces coelicolor	? + oxidized ferredoxin [iron-sulfur] cluster + H2O	about 70fold lower activity than with flaviolin	?
1.14.19.69	4 flaviolin + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H+ + O2	-	Streptomyces coelicolor	3,3'-biflaviolin + 3,8'-biflaviolin + 4 oxidized ferredoxin [iron-sulfur] cluster + 4 H2O	-	?

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Release 2023.1 (January 2023)