Electron paramagnetic resonance studies of ferric cytochrome c' from photosynthetic bacteria.
Electronic ground nature of ferric cytochromes c' isolated from five photosynthetic bacteria. Chromatium vinosum ATCC 17899, Rhodobacter capsulatus ATCC 11166, Rhodopseudomonas palustris ATCC 17001, Rhodospirillum molischianum ATCC 14031, and Rhodospirillum rubrum ATCC 11170 has been investigated by electron paramagnetic resonance (EPR) spectroscopy. EPR spectra indicate that the electronic ground state of five ferric cytochromes c' is a quantum mechanical admixed-spin state of a high spin (S = 5/2) and an intermediate spin (S = 3/2) at pH 7.2 and is high-spin state at pH 11.0. At physiological pH, however, the content of an intermediate spin state differs with the bacterial source of the protein: approximately 50%, Chromatium vinosum; approximately 40%, Rhodobacter capsulatus and Rhodopseudomonas palustris; approximately 10%, Rhodospirillum molischianum and Rhodospirillum rubrum. Computer simulation of the spectra supports this diversity of the contribution of an intermediate spin state. Model studies of the ferric porphyrin complexes suggest that the correlation between content of an intermediate spin state and heme iron displacement from the mean heme plane. Therefore, the variation of the content of an intermediate spin state observed in the present study reflects the subtle difference in the degree of heme iron displacement among the proteins.
Fujii
S
S
Institute for Life Support Technology, Yamagata Technopolis Foundation, Japan.
Yoshimura
T
T
Kamada
H
H
Yamaguchi
K
K
Suzuki
S
S
Shidara
S
S
Takakuwa
S
S
D002844:Chromatium / Q000201:enzymology*; D003578:Cytochrome-c Peroxidase / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D006863:Hydrogen-Ion Concentration; D010544:Peroxidases / Q000737:chemistry* / Q000302:isolation & purification; D016354:Rhodobacter capsulatus / Q000201:enzymology*; D012241:Rhodopseudomonas / Q000201:enzymology*; D012246:Rhodospirillum / Q000201:enzymology*
D010544:Peroxidases; C021799:microperoxidase; D003578:Cytochrome-c Peroxidase