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 | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces coelicolor | - |
isoform CYP158A2 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | ? | |
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 | - |
? |