Characterization by EPR spectroscopy of cytochrome b-562 isolated from the cytochrome b-c1 complex of Rhodopseudomonas sphaeroides R-26

Koh Iba, Ken Ichiro Takamiya, Shigeru Itoh

Research output: Contribution to journalArticle

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Abstract

The EPR spectra of cytochrome b-562 isolated from the cytochrome b-c1 complex of Rhodopseudomonas sphaeroides were measured at liquid helium temperature. The purified cytochrome b-562 gives a high spin signal at g=6.0. Anaerobic titration of this signal confirmed the presence of two redox components with Em=40 and -110 mV at pH 7.5. These values are consistent with the published ones, Em= 55 and -100 mV at pH 7.0, that were optically estimated for the same type of preparation (Iba et al. (1985) FEBS Lett. 183, 151-154). The power saturation behavior of the g= 6.0 signal at different redox potentials indicated a direct spin-spin interaction between these two redox centers.

Original languageEnglish
Pages (from-to)1477-1480
Number of pages4
JournalJournal of biochemistry
Volume100
Issue number6
DOIs
Publication statusPublished - Oct 1 1986

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Cytochromes c1
Rhodobacter sphaeroides
Cytochromes b
Oxidation-Reduction
Paramagnetic resonance
Spectrum Analysis
Spectroscopy
Helium
Titration
Temperature
Liquids

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Cite this

Characterization by EPR spectroscopy of cytochrome b-562 isolated from the cytochrome b-c1 complex of Rhodopseudomonas sphaeroides R-26. / Iba, Koh; Takamiya, Ken Ichiro; Itoh, Shigeru.

In: Journal of biochemistry, Vol. 100, No. 6, 01.10.1986, p. 1477-1480.

Research output: Contribution to journalArticle

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