Most energy-transducing membranes contain a bc-type complex such as the cytochrome bc 1 complex or the cytochrome b 6 f complex. Members of this family couple electron transfer and proton translocation across the membrane. They also share some structural homologies, having three redox-active subunits in common: the Rieske iron-sulfur protein, a b-type cytochrome (cytochrome b or b 6 ), and a c-type cytochrome (cytochrome c 1 or f). Moreover, there is sequence homology between cytochrome b 6 , subunit IV, and the Rieske protein of the b 6 f complex, and the N-and C-terminal parts of cytochrome b, and the Rieske protein of the bc 1 complex, respectively. Cytochrome c 1 and cytochrome f, on the other hand, do not share any sequence homology. Spectroscopic and EPR properties of the hemes and of the iron-sulfur cluster are similar, although not identical, and some inhibitors affect both complexes equally (reviewed in Refs. 4 -7).The b 6 f complex is found in the thylakoid membrane of higher plants and algae and in the membrane of some cyanobacteria (for reviews, see . Besides the four high molecular weight subunits mentioned above, the b 6 f complex comprises four smaller subunits, PetG, PetL, PetM, and , that have no direct counterpart in the bc 1 complex. The cytochrome b 6 f is the middle component of the photosynthetic chain, coupling the electron transfer from photosystem II (via plastoquinol) to photosystem I (via plastocyanin or a c-type cytochrome).The most widely accepted mechanism for the bc-type complexes is the so-called "Q-cycle" mechanism proposed by Mitchell (18) and modified by Crofts et al. (19). According to this model, two electron paths are distinguished within the complex as follows: a high potential chain, composed of the iron-sulfur cluster of the Rieske protein and the heme of the c-type heme, and a low potential chain, composed of the two hemes of the b-type cytochrome, the low potential b L and high potential b H hemes. Two quinol/quinone-binding sites, located on opposite sides of the membrane, are also predicted: the Q o site, on the intermembrane space/lumenal side of the membrane, and the Q i site, on the matrix/stromal side of the membrane. A turnover of the Q o site comprises the oxidation of a two-electron carrier quinol, one electron reducing the Rieske protein, which in turn reduces the c-type cytochrome and which ultimately reduces plastocyanin or cytochrome c, and the other electron reducing b L , which in turn is oxidized by b H . These events are associated with the release of two protons in the intermembrane space/ lumen. A second turnover reduces another plastocyanine molecule and places both hemes of the b-type cytochrome in a reduced state. The reduction of a quinone at the Q i site results in the oxidation of the two b hemes and an uptake of two protons from the matrix/stroma. Thus, these complexes contribute to generating the proton gradient that drives ATP synthesis in respiration and photosynthesis.Recently, the structure of several bc 1 complexes from mitochondria have ...
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