Spectroscopic features of cytochrome P450 reaction intermediates

Production of alkenes and novel secondary products by P450 OleTJE using novel H2O2‐generating fusion protein systems

“…8456 OleT JE (CYP152L1) is a member of the cytochrome P450 (P450 or CYP) enzyme superfamily. P450s bind heme b, which is proximally coordinated by a cysteine thiolate and typically has a water ligand in the 6 th position in the resting state (1). Substrate binding generally displaces the distal water ligand, converting low-spin (LS) ferric heme iron to the high-spin (HS) state (2).…”

Cytochrome P450 Is Present in Both Ferrous and Ferric Forms in the Resting State within Intact Escherichia coli and Hepatocytes

“…The resting state of P450s is typically portrayed as the ferric form in representations and descriptions of the P450 catalytic cycle (5)(6)(7)(11)(12)(13)(14). To our knowledge, no experimental evidence exists that addresses the in vivo oxidation state of P450s.…”

Human Cytochrome P450 17A1 Conformational Selection

“…Spectroscopy and other biophysical methods have been powerful approaches to probe P450 catalysis, leading to the current understanding of the catalytic cycle (12,13). However, the present compendium of mammalian P450 x-ray structures represents only the first substrate-binding step in a multistep catalytic cycle.…”