The origin of the low-spin character of the resting state of cytochrome P450cam investigated by means of active site analogues.
Crown-capped iron(S-) porphyrins 1 x H2O and 2 x H2O and their corresponding Ba2+ complexes have been prepared as active site analogues of the resting state of cytochrome P450cam. cw-EPR studies and electronic structure calculations at the density functional theory (DFT) level of model systems suggest a functional role of the water cluster of P450cam.
Lochner
Martin
M
Department of Chemistry, University of Basel, St. Johanns-Ring 19, 4056 Basel, Switzerland.
Meuwly
Markus
M
Woggon
Wolf D
WD
D017609:Barium Compounds / Q000138:chemical synthesis / Q000737:chemistry; D001665:Binding Sites; D019475:Camphor 5-Monooxygenase / Q000737:chemistry*; D043844:Crown Ethers / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D006418:Heme / Q000737:chemistry; D006860:Hydrogen Bonding; D007202:Indicators and Reagents; D007501:Iron / Q000737:chemistry; D008956:Models, Chemical; D010084:Oxidation-Reduction; D012997:Solvents; D013455:Sulfur / Q000737:chemistry; D014867:Water / Q000737:chemistry
D017609:Barium Compounds; D043844:Crown Ethers; D007202:Indicators and Reagents; D012997:Solvents; D014867:Water; D006418:Heme; D013455:Sulfur; D007501:Iron; D019475:Camphor 5-Monooxygenase