ISSN:
1573-6881
Keywords:
QO site
;
ubiquinone binding
;
electron paramagnetic resonance
;
inhibitors
;
electron transfer
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Physics
Notes:
Abstract The primary energy conversion (QO) site of the cytochrome bc 1 complex is flanked by bothhigh- and low-potential redox cofactors, the [2Fe–2S] cluster and cytochrome b L, respectively.From the sensitivity of the reduced [2Fe–2S] cluster electron paramagnetic resonance (EPR)spectral g x-band and line shape to the degree and type of QO site occupants, we have proposeda double-occupancy model for the QO site by ubiquinone in Rhodobacter capsulatus membranevesicles containing the cytochrome bc 1 complex. Biophysical and biochemical experimentshave confirmed the double occupancy model and from a combination of these results and theavailable cytochrome bc 1 crystal structures we suggest that the two ubiquinone molecules inthe QO site serve distinct catalytic roles. We propose that the strongly bound ubiquinone,termed QOS, is close to the [2Fe–2S] cluster, where it remains tightly associated with the QOsite during turnover, serving as a catalytic cofactor; and the weaker bound ubiquinone, QOW,is distal to the [2Fe–2S] cluster and can exchange with the membrane Qpool on a time scalemuch faster than the turnover, acting as the substrate. The crystallographic data demonstratesthat the FeS subunit can adopt different positions. Our own observations show that theequilibrium position of the reduced FeS subunit is proximal to the QO site. On the basis of this, wealso report preliminary results modeling the electron transfer reactions that can occur in thecytochrome bc 1 complex and show that because of the strong distance dependence of electrontransfer, significant movement of the FeS subunit must occur in order for the complex to beable to turn over at the experimental observed rates.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1005467628660
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