Thermodynamic and spectroscopic characteristics of the cytochrome bc1 complex. Role of quinone in the behavior of cytochrome b562

J. C. Salerno, Yan Xu, M. P. Osgood, C. H. Kim, T. E. King

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Abstract

Cytochrome b562 does not behave as a single independent thermodynamic component in preparations of purified quinol cytochrome c reductase. This effect is much more pronounced in quinone sufficient preparations; in such preparations, the epr spectrum of the cytochrome is E(h) sensitive, with a peak shift from g = 3.42 to 3.48 occurring as the potential is lowered from 100 mV to 0 mV. The peak shift is dependent on the presence of quinone and can be restored to quinone-depleted preparations by supplementation with ubiquinol 2 if phospholipid depletion is not too severe. The results suggest that cytochrome b562 is strongly interacting with the Qc quinone binding site.

Original languageEnglish (US)
Pages (from-to)15398-15403
Number of pages6
JournalJournal of Biological Chemistry
Volume264
Issue number26
StatePublished - 1989
Externally publishedYes

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Electron Transport Complex III
Cytochromes
Thermodynamics
Hydroquinones
Cytochrome Reductases
Cytochromes c
Phospholipids
Oxidoreductases
Binding Sites
benzoquinone

ASJC Scopus subject areas

  • Biochemistry

Cite this

Thermodynamic and spectroscopic characteristics of the cytochrome bc1 complex. Role of quinone in the behavior of cytochrome b562 . / Salerno, J. C.; Xu, Yan; Osgood, M. P.; Kim, C. H.; King, T. E.

In: Journal of Biological Chemistry, Vol. 264, No. 26, 1989, p. 15398-15403.

Research output: Contribution to journalArticle

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AU - King, T. E.

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