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Literature summary for 1.14.19.69 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.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Streptomyces coelicolor
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isoform CYP158A2
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Substrates and Products (Substrate)

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