Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Zhu, Q.S. et al.

Reduction of exogenous quinones and 2,6-dichlorophenol indophenol in cytochrome b-deficient yeast mitochondria: a differential effect on center i and center o of the cytochrome b-c1 complex.

The reduction of duroquinone (DQ), 2,3-dimethoxy-5-methyl-6-decyl-1,4-benzoquinone (DB), and dichlorophenol indophenol (DCIP) by succinate and NADH was investigated in yeast mitochondria which have no spectrally detectable cytochrome b. Succinate reduces DB in the cytochrome b-deficient mitochondria at rates comparable to that observed in wild-type mitochondria, suggesting that succinate:ubiquinone oxidoreductase is unaffected by the lack of cytochrome b. In the mutant mitochondria, succinate does not reduce DQ or DCIP at significant rates; however, NADH reduces both DQ and DCIP at rates similar to that of the wild-type mitochondria in a myxothiazol, but not antimycin, sensitive reaction. The Ki for myxothiazol in this reaction is close to that for electron transfer through the cytochrome b-c1 complex. In addition, myxothiazol does not inhibit NADH:ubiquinone oxidoreductase. These results confirm our previous suggestion that the cytochrome b-c1 complex is involved in electron transfer from the primary dehydrogenases to DQ and DCIP and suggest that cytochrome b is not the binding site for myxothiazol.[1]

References

Reduction of exogenous quinones and 2,6-dichlorophenol indophenol in cytochrome b-deficient yeast mitochondria: a differential effect on center i and center o of the cytochrome b-c1 complex. Zhu, Q.S., Sprague, S.G., Beattie, D.S. Arch. Biochem. Biophys. (1988) [Pubmed]

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