Abstract
Resonance Raman scattering excitation profile data have been obtained on ferrocytochromes c and b5 in the alpha absorption band region. We observe in cytochrome c that the shape of the excitation profile agrees with the absorption band shape, while in cytochrome b5 it does not. In addition, we observe in cytochrome b5 a linewidth substantially larger than that in cytochrome c. From our data we conclude that the excited state lifetime in cytochrome c is longer than that in cytochrome b5 and that in cytochrome b5 the relaxation of the pi-pi* excited state configuration of the porphyrin ring is different in the x direction than in the y direction. Possible origins of these effects due to coupling to the d-d transitions of the iron atom are discussed.
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Selected References
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