1.2.5.1	malfunction	inactivation of the pyruvate:quinone oxidoreductase results in a more efficient L-valine production in Corynebacterium glutamicum strain aceE A16	-, 724036	
1.2.5.1	malfunction	there is a positive effect on L-valine production by the inactivation of the pyruvate:quinone oxidoreductase due to increased pyruvate availability	-, 724069	
1.2.5.1	physiological function	electron transport from pyruvate to oxygen in the liposome system generates a trans-membrane potential of at least 180 mV, negative inside, which is sensitive to the uncouplers carbonyl cyanide p-(trichloromethoxy)phenylhydrazone and valinomycin. A transmembrane potential is also generated by the oxidation of ubiquinol 1 by the terminal oxidase in the absence of the flavoprotein. The pyruvate oxidase can directly reduce ubiquinone 8 within the phospholipid bilayer, menaquinone 8 will not effectively substitute for ubiquinone 8 in this electron-transfer chain, and the cytochrome d terminal oxidase functions as a ubiquinol 8 oxidase and serves as a coupling site in the Escherichia coli aerobic respiratory chain	702185	
1.2.5.1	physiological function	inactivation of the chromosomal pqo gene leads to the absence of pyruvate:quinone oxidoreductase activity. Growth and amino acid production are not affected under either condition tested. Introduction of plasmid-bound pqo into a pyruvate dehydrogenase complex-negative strain partially relieves the growth phenotype of this mutant, indicating that high pyruvate:quinone oxidoreductase activity can compensate for the function of the pyruvate dehydrogenase complex	704267	
1.2.5.1	physiological function	the activated enzyme can be efficiently regulated by the oxidation level of the quinone pool in natural membranes	702204	
1.2.5.1	physiological function	the cytochrome o complex functions as an efficient ubiquinol-8 oxidase in reconstituted proteoliposomes, and ubiquinone-8 serves as an electron carrier from the flavoprotein pyruvate oxidase to the cytochrome complex. Electron flow from the flavoprotein to oxygen in the reconstituted proteoliposomes generates a transmembrane potential of at least 120 mV, negative inside, which is sensitive to ionophore uncouplers and inhibitorso f the terminal oxidase. The minimal composition of this respiratory chain is a flavoprotein dehydrogenase, ubiquinone-8, and the cytochrome o complex	704373