Cocchi S, Zannoni D
Arch Microbiol. 1985 Sep;142(4):365-9. doi: 10.1007/BF00491905.
Myxothiazol inhibited the electron transport in the cytochrome b/c segment of membrane particles from Pseudomonas cichorii. A residual NADH-oxidation due to the presence of an alternative pathway via cytochrome o (Em, 7 = +250 mV) was sensitive to the quinone analog 5-undecyl-6-hydroxy-4,7-dioxobenzothiazole (UHDBT). This latter inhibitor was equally effective in blocking the linear respiratory chain of Pseudomonas aptata, a strain deficient in cytochromes of c type and Rieske iron-sulphur centre. The analysis of the oxido-reduction kinetic patterns of cytochromes indicated that, among the b type haems present in P. aptata, only cyt. o could be reduced by ubiquinol-1 in a reaction insensitive to both antimycin A and myxothiazol but inhibited by UHDBT. This latter finding has been correlated to the fact that P. aptata exhibits a defective b/c complex. In membranes from P. cichorii, in which the absorption maximum of dithionite reduced cytochrome(s) b shifted by 2-3 nm in the presence of antimycin A and/or myxothiazol, the electron flow through the b/c oxidoreductase complex has tentatively been arranged in a proton motive "Q-cycle" like mechanism.