The specificity of mitochondrial complex I for ubiquinones
Esposti, Mauro, Ngo, Anna, McMullen, Gabrielle, Ghelli, Anna, Sparla, Francesca, Benelli, Bruna, Ratta, Marina and Linnane, Anthony Williams. (1996). The specificity of mitochondrial complex I for ubiquinones. Biochemical Journal. 313(1), pp. 327 - 334. https://doi.org/10.1042/bj3130327
|Esposti, Mauro, Ngo, Anna, McMullen, Gabrielle, Ghelli, Anna, Sparla, Francesca, Benelli, Bruna, Ratta, Marina and Linnane, Anthony Williams
We report the first detailed study on the ubiquinone (coenzyme Q; abbreviated to Q) analogue specificity of mitochondrial complex I, NADH:Q reductase, in intact submitochondrial particles. The enzymic function of complex I has been investigated using a series of analogues of Q as electron acceptor substrates for both electron transport activity and the associated generation of membrane potential. Q analogues with a saturated substituent of one to three carbons at position 6 of the 2,3-dimethoxy-5-methyl-1,4-benzoquinone ring have the fastest rates of electron transport activity, and analogues with a substituent of seven to nine carbon atoms have the highest values of association constant derived from NADH:Q reductase activity. The rate of NADH:Q reductase activity is potently but incompletely inhibited by rotenone, and the residual rotenone-insensitive rate is stimulated by Q analogues in different ways depending on the hydrophobicity of their substituent. Membrane potential measurements have been undertaken to evaluate the energetic efficiency of complex I with various Q analogues. Only hydrophobic analogues such as nonyl-Q or undecyl-Q show an efficiency of membrane potential generation equivalent to that of endogenous Q. The less hydrophobic analogues as well as the isoprenoid analogue Q-2 are more efficient as substrates for the redox activity of complex I than for membrane potential generation. Thus the hydrophilic Q analogues act also as electron sinks and interact incompletely with the physiological Q site in complex I that pumps protons and generates membrane potential.
|313 (1), pp. 327 - 334
|Portland Press Ltd.
|Digital Object Identifier (DOI)
|327 - 334
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