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 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
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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 journal › Article
}
TY - JOUR
T1 - Thermodynamic and spectroscopic characteristics of the cytochrome bc1 complex. Role of quinone in the behavior of cytochrome b562
AU - Salerno, J. C.
AU - Xu, Yan
AU - Osgood, M. P.
AU - Kim, C. H.
AU - King, T. E.
PY - 1989
Y1 - 1989
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0024432573&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0024432573&partnerID=8YFLogxK
M3 - Article
C2 - 2549062
AN - SCOPUS:0024432573
VL - 264
SP - 15398
EP - 15403
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 26
ER -