A Role for Active Site Water Molecules and Hydroxyl Groups of Substrate for Oxygen Activation in Cytochrome P450 158A2

Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer

Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2

MTEETISQAVPPVRDWPAVDLPGSDFDPVLTELMREGPVTRISLPNGEGWAWLVTRHDDVRLVTNDPRFGREAVMDRQVT
RLAPHFIPARGAVGFLDPPDHTRLRRSVAAAFTARGVERVRERSRGMLDELVDAMLRAGPPADLTEAVLSPFPIAVICEL
MGVPATDRHSMHTWTQLILSSSHGAEVSERAKNEMNAYFSDLIGLRSDSAGEDVTSLLGAAVGRDEITLSEAVGLAVLLQ
IGGEAVTNNSGQMFHLLLSRPELAERLRSEPEIRPRAIDELLRWIPHRNAVGLSRIALEDVEIKGVRIRAGDAVYVSYLA
ANRDPEVFPDPDRIDFERSPNPHVSFGFGPHYCPGGMLARLESELLVDAVLDRVPGLKLAVAPEDVPFKKGALIRGPEAL
PVTWAAA

PEG 3350, flaviolin, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K

The same protein complexed with two molecules of flaviolin

The same protein complexed with 4-phenylimidazole

structure refinement with starting model

streptomyces, Cytochrome P450 oxidoreductase, CYP158A2, proton transfer, dioxygen activation, Oxidoreductase

MTEETISQAVPPVRDWPAVDLPGSDFDPVLTELMREGPVTRISLPNGEGWAWLVTRHDDVRLVTNDPRFGREAVMDRQVT
RLAPHFIPARGAVGFLDPPDHTRLRRSVAAAFTARGVERVRERSRGMLDELVDAMLRAGPPADLTEAVLSPFPIAVICEL
MGVPATDRHSMHTWTQLILSSSHGAEVSERAKNEMNAYFSDLIGLRSDSAGEDVTSLLGAAVGRDEITLSEAVGLAVLLQ
IGGEAVTNNSGQMFHLLLSRPELAERLRSEPEIRPRAIDELLRWIPHRNAVGLSRIALEDVEIKGVRIRAGDAVYVSYLA
ANRDPEVFPDPDRIDFERSPNPHVSFGFGPHYCPGGMLARLESELLVDAVLDRVPGLKLAVAPEDVPFKKGALIRGPEAL
PVTW