Abstract
In this minireview an overview is presented of the kinetics of electron transfer within the cytochrome bc 1 complex, as well as from cytochrome bc 1 to cytochrome c. The cytochrome bc 1 complex (ubiquinone:cytochrome c oxidoreductase) is an integral membrane protein found in the mitochondrial respiratory chain as well as the electron transfer chains of many respiratory and photosynthetic bacteria. Experiments on both mitochondrial and bacterial cyatochrome bc 1 have provided detailed kinetic information supporting a Q-cycle mechanism for electron transfer within the complex. On the basis of X-ray crystallographic studies of cytochrome bc 1, it has been proposed that the Rieske iron–sulfur protein undergoes large conformational changes as it transports electrons from ubiquinol to cytochrome c 1. A new method was developed to study electron transfer within cytochrome bc 1 using a binuclear ruthenium complex to rapidly photooxidize cytochrome c 1. The rate constant for electron transfer from the iron–sulfur center to cytochrome c 1 was found to be 80,000 s−1, and is controlled by the dynamics of conformational changes in the iron–sulfur protein. Moreover, a linkage between the conformation of the ubiquinol binding site and the conformational dynamics of the iron–sulfur protein has been discovered which could play a role in the bifurcated oxidation of ubiquinol. A ruthenium photoexcitation method has also been developed to measure electron transfer from cytochrome c 1 to cytochrome c. The kinetics of electron transfer are interpreted in light of a new X-ray crystal structure for the complex between cytochrome bc 1 and cytochrome c.
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Millett, F., Durham, B. Kinetics of Electron Transfer within Cytochrome bc 1 and Between Cytochrome bc 1 and Cytochrome c . Photosynthesis Research 82, 1–16 (2004). https://doi.org/10.1023/B:PRES.0000040434.77061.ca
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DOI: https://doi.org/10.1023/B:PRES.0000040434.77061.ca