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- W2053845615 abstract "We have measured the resonance Raman excitation profiles (REP’s) of several vibrational modes associated with the heme active site of cytochrome P450cam. The important Fe–S axial ligand mode (351 cm−1) of the substrate bound (high‐spin ferric) complex is found to have structure in its blue shifted REP. Inverse transform techniques allow the line shape of the resonant charge transfer absorption to be reconstructed directly from the REP data. The observed splitting (3200 cm−1) is associated with an inequivalence in the resonant S→Fe charge transfer excitations. The position of the high‐energy component (∼323 nm) is found to be in excellent agreement with z‐polarized single crystal measurements, while the low‐energy component (∼360 nm) is not clearly observed in the single crystal analysis. The ‘‘spin‐marker’’ band ν3 is found to have a REP that is significantly red shifted with respect to the theoretical predictions. A variety of perturbations including non‐Condon and multiple state coupling, as well as sta..." @default.
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- W2053845615 date "1987-10-15" @default.
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- W2053845615 title "Investigations of the resonance Raman excitation profiles of cytochromeP450cam" @default.
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- W2053845615 doi "https://doi.org/10.1063/1.452885" @default.
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