The three-subunit cytochrome bc1 complex of Paracoccus denitrificans. Its physiological function, structure, and mechanism of electron transfer and energy transduction.

The cytochrome bc1 complex purified from P. denitrificans has the same electron-transfer and energy-transducing activities, is sensitive to the same electron-transfer inhibitors, and contains cytochromes b, c1, iron-sulfur protein, and thermodynamically stable ubisemiquinone identical to the counterpart complexes from mitochondria. However, the bacterial bc1 complex consists of only three proteins, the obligate electron-transfer proteins, while the mitochondrial complexes contain six or more supernumerary polypeptides, which have no obvious electron-transfer function. The P. denitrificans complex is a paradigm for the bc1 complexes of all gram-negative bacteria. In addition, because of its simple polypeptide composition and apparently minimal damage during isolation, the P. denitrificans bc1 complex is an ideal system in which to study structure-function relationships requisite to energy transduction linked to electron transfer.