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• W1996869512 abstract "Resonance Raman spectra have been obtained for cytochrome c′ from Rhodopseudomonas palustris, using laser excitation frequencies in the region of both the Soret band and the α-β bands. The porphyrin-ring vibrational frequencies are compared with those of other heme proteins which are in well-defined spin and oxidation states. In alkaline solution (pH > 11.5) both oxidized and reduced forms show normal low-spin heme vibrational patterns. At lower pH the reduced form (high spin) shows a pattern similar to that of deoxyhemoglobin, i.e. that of a high-spin five-coordinate ferroheme. The lower pH forms of the oxidized protein exhibit anomalous spectra, with frequencies which are closer to expected low-spin than high-spin values, although their magnetic moments, while intermediate, are closer to expected high-spin values. Mixtures of high- and low-spin forms can be ruled out by the absence of two sets of vibrational frequencies, which are seen for hydroxymethemoglobin, an authentic mixed-spin heme protein. It is suggested that the heme groups are closer to being planar than are normal high-spin hemes, and that the spin state may be intermediate, s = 32. At pH 10.3 the inferred structure is less planar than at pH 6.9, consistent with trends in the absorption spectrum. The depolarization ratios of the polarized approx. 1370-cm−1 Raman band indicate a lowering of 4-fold symmetry of the heme chromophore in the lower pH forms of both oxidized and reduced cytochrome c′, consistent with the observed splittings of the Soret band." @default.
• W1996869512 created "2016-06-24" @default.
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• W1996869512 date "1974-06-01" @default.
• W1996869512 modified "2023-10-15" @default.
• W1996869512 title "Resonance-Raman evidence for anomalous heme structures in cytochrome c′ from Rhodopseudomonas palustris" @default.
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• W1996869512 doi "https://doi.org/10.1016/0005-2795(74)90186-x" @default.
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