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 language | English (US) |
|---|---|
| Pages (from-to) | 15398-15403 |
| Number of pages | 6 |
| Journal | Journal of Biological Chemistry |
| Volume | 264 |
| Issue number | 26 |
| State | Published - 1989 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology
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Salerno, J. C., Xu, Y., Osgood, M. P., Kim, C. H., & King, T. E. (1989). Thermodynamic and spectroscopic characteristics of the cytochrome bc1 complex. Role of quinone in the behavior of cytochrome b562. Journal of Biological Chemistry, 264(26), 15398-15403.