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The three-subunit cytochromebc 1 complex ofParacoccus denitrificans. Its physiological function, structure, and mechanism of electron transfer and energy transduction

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Abstract

The cytochromebc 1 complex purified fromP. denitrificans has the same electron-transfer and energy-transducing activities, is sensitive to the same electron-transfer inhibitors, and contains cytochromesb, c 1, iron-sulfur protein, and thermodynamically stable ubisemiquinone identical to the counterpart complexes from mitochondria. However, the bacterialbc 1 complex consists of only three proteins, the obligate electron-transfer proteins, while the mitochondrial complexes contain six or more supernumerary poly-peptides, which have no obvious electron-transfer function. TheP. denitrificans complex is a paradigm for thebc 1 complexes of all gram-negative bacteria. In addition, because of its simple polypeptide composition and apparently minimal damage during isolation, theP. denitrificans bc 1 complex is an ideal system in which to study structure-function relationships requisite to energy transduction linked to electron transfer.

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  1. Department of Biochemistry, Dartmouth Medical School, 03756, Hanover, New Hampshire

    Bernard L. Trumpower

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  1. Bernard L. Trumpower
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Trumpower, B.L. The three-subunit cytochromebc 1 complex ofParacoccus denitrificans. Its physiological function, structure, and mechanism of electron transfer and energy transduction. J Bioenerg Biomembr 23, 241–255 (1991). https://doi.org/10.1007/BF00762220

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