Premium
Resonance Raman scattering of cytochrome P450 BM3 and effect of imidazole inhibitors
Author(s) -
Smith S. J.,
Munro A. W.,
Smith W. E.
Publication year - 2003
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10502
Subject(s) - chemistry , imidazole , raman spectroscopy , resonance raman spectroscopy , resonance (particle physics) , hemeprotein , raman scattering , heme , steric effects , ring (chemistry) , nuclear magnetic resonance , photochemistry , crystallography , stereochemistry , optics , organic chemistry , atomic physics , physics , enzyme
Resonance Raman scattering from cytochrome P450 BM3 is obtained with a Raman microprobe using 406‐nm excitation with an accumulation time of a few seconds. The small sample size and rapid measurement time make the routine characterization of P450 systems by resonance Raman spectroscopy easier. Addition of imidazole and imidazole derivatives as inhibitors causes the appearance of additional peaks due to vinyl modes, increases the relative intensity of symmetric modes that would be A 1g in D 4h symmetry, and causes a large drop in the intensity of ν 11 . This information indicates that the ligation of imidazoles to the heme iron causes the alignment of the vinyl modes with the plane of the heme ring and reduces the out of plane distortion of the ring. The effect of both inhibitors is similar but there is a subtle difference in the extent of the reduction in the intensity of ν 11 , which suggests that steric effects within the pocket are having some effect. © 2003 Wiley Periodicals, Inc. Biopolymers (Biospectroscopy) 70: 620–627, 2003