Localization and mobility of coenzyme Q in lipid bilayers and membranes

We have studied the mobility of coenzyme Q (CoQ) in lipid bilayers and mitochondrial membranes in relation to the control of electron transfer activities. A molecular dynamics computer simulation in the vacuum yielded a folded structure for CoQ(10), with a length of only 21 Angstrom. Using this information we were able to calculate diffusion coefficients in the range of 10(-6) cm(2)/s in good agreement with those found experimentally by fluorescence quenching of pyrene derivatives. To investigate if CoQ diffusion may represent the rate-limiting step of electron transfer, we reconstituted complexes I and III and assayed the resulting NADH cytochrome c reductase activity in presence of different CoQ(10) levels and at different distances between complexes; the experimental turnovers were higher than the collision frequencies calculated using diffusion coefficients of 10(-9) cm(2)/s but compatible with values found by us by fluorescence quenching. Since;the experimental turnovers are independent of the distance between complexes, we conclude that CoQ diffusion is not rate-limiting for electron transfer.