A mutant of Paracoccus denitrificans which is deficient in c-type cytochromes grows aerobically with generation times similar to those obtained with a wild-type strain. The aa3-type oxidase is functional in the mutant as judged by spectrophotometric assays of cytochrome c oxidation using the membrane particles and cytochrome aa3reduction in whole cells. The cytochrome c oxidase (aa3-type) of the c-less mutant oxidizes soluble cytochrome c at rates equivalent to those obtained with the wild-type. NADH and succinate oxidase activities of the membrane preparations of the mutant and wild-type are also comparable in the absence of detergent treatment. Exogenous soluble cytochrome c can be both reduced by NADH- and succinate-linked systems and oxidized by cytochrome aa3present in membranes of the mutant strain. Rapid overall electron transport can occur in the c-less mutant, suggesting that reactions result from collision of diffusing complexes. © 1989 Elsevier Science Publishers B.V. (Biomedical Division) All rights reserved.
Bolgiano, B., Smith, L., & Davies, H. C. (1989). Electron transport reactions in a cytochrome c-deficient mutant of Paracoccus denitrificans. BBA - Bioenergetics, 973(2), 227–234. https://doi.org/10.1016/S0005-2728(89)80426-8