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Spectral properties of cytochrome c' from Rhodopseudomonas capsulata B100 and its CO complex.

Authors
  • Yoshimura, T
  • Suzuki, S
  • Iwasaki, H
  • Takakuwa, S
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Apr 14, 1987
Volume
144
Issue
1
Pages
224–231
Identifiers
PMID: 3034243
Source
Medline
License
Unknown

Abstract

The spectral properties of cytochrome c' from photosynthetic bacterium Rhodopseudomonas capsulata (= Rhodobacter capsulatus) B100 and its CO complex are reported. The electronic absorption, MCD, and EPR spectra have been compared with those of the other cytochromes c' and horse heart cytochrome c. EPR and electronic spectral results for the ferric cytochrome c' suggest that the ground state of heme-iron(III) at neutral pH consists of a quantum mechanical admixture of an intermediate-spin and a high-spin state and that at pH 11.0 is in a high-spin state. In the MCD spectrum of the CO-ferrous cytochrome c', the MCD intensity in the Soret band region was much higher than that of CO complexes of hemoproteins with a protoheme. The differences in a stereochemistry of the sixth-coordination position is discussed.

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