| 6536673 |
Landi L, Pasquali P, Cabrini L, Sechi AM, Lenaz G: On the mechanism of inhibition of NADH oxidase by ubiquinone-3. Am J Physiol Cell Physiol. 2007 Feb;292(2):C719-28. Epub 2006 Oct 18.
The combined effects of rotenone and ubiquinone-3 on the kinetics of NADH dehydrogenase and NADH oxidase have been investigated. The two inhibitors do not show additivity; on the other hand, ubiquinone-3, when preincubated with the enzyme, partially removes rotenone sensitivity. The inhibition of NADH oxidase by ubiquinone-3 is the result of at least two combined effects: the competition of the less active ubiquinone-3 with endogenous ubiquinone-10 in the acceptor site of the dehydrogenase, and a nonspecific action on the structure of complex I. The latter effect is perhaps mediated by a physical change of the phospholipid bilayer similar to that observed with agents such as butanol, perturbing lipid-protein interactions in the membrane. |
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