Abstract
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 A1g, in D4h symmetry, and causes a large drop in the intensity of ν11. 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 ν11, which suggests that steric effects within the pocket are having some effect. © 2003 Wiley Periodicals, Inc.
Original language | English |
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Pages (from-to) | 620-627 |
Number of pages | 7 |
Journal | Biopolymers |
Volume | 70 |
Issue number | 4 |
DOIs | |
Publication status | Published - Dec 2003 |
Keywords
- Cytochrome P450 enzymes
- Inhibitor interaction
- Resonance Raman scattering