Abstract
According to the chemiosmotic theory of Mitchell, generation of the transmembrane proton gradient is the result of electron flow through a series of membrane-bound electron carriers1. These multisubunit complexes, which can be isolated as distinct, functional entities, are interconnected via small electron carriers, like quinones and cytochrome c. The ubiquinol:cytochrome c oxidoreductase (or the cytochrome bc 1 complex), is one of the most common example of these complexes. It is responsible for the transfer of electrons from ubiquinol to cytochrome c, a central step in respiratory and photosynthetic energy transduction pathways, while in doing so it translocates protons across the impermeable membrane. The proton gradient and the membrane potential thus established are then used for cellular functions like ATP production and transport. Cytochrome bc 1 complexes are present in many prokaryotes, including photosynthetic bacteria, and in mitochondria of eukaryotes. A similar structure, the cytochrome b 6 /f complex, also exists in chloroplasts of plants. Although the subunit compositions of these complexes vary according to their origin, the essential redox-active components, cytochromes b and c1, Rieske Fe-S protein and ubiquinone, are always conserved2.
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Daldal, F. (1987). Molecular Genetic Approaches to Studying the Structure and Function of the Cytochrome c 2 and the Cytochrome bc 1 Complex from Rhodobacter Capsulatus . In: Papa, S., Chance, B., Ernster, L. (eds) Cytochrome Systems. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1941-2_3
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DOI: https://doi.org/10.1007/978-1-4613-1941-2_3
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