Correlations between structural and spectroscopic properties of the high-spin heme protein cytochrome c'

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Abstract
The cytochromes c'' are a class of heme proteins whose native spectroscopic properties have been suggested to represent a quantum mechanical admixture of intermediate-(S = 3/2) and high- (S = 5/2) spin states. Here features of the cytochrome c'' heme environment, as revealed by X-ray crystallographic studies of the dimeric cytochrome c'' from Rhodospirillum molischianum, are related to the observed spectroscopic properties. The environment of the heme group in cytochrome c'' supports the existence of the admixed spin state at neutral pH and suggests that pH-dependent transition to a pure high-spin state at alkaline pH involves deprotonation of the histidine axial ligand to the heme Fe.

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