Quinone specificity of complex I.
This review considers the interaction of Complex I with different redox acceptors, mainly homologs and analogs of the physiological acceptor, hydrophobic Coenzyme Q. After examining the physical properties of the different quinones and their efficacy in restoring mitochondrial respiration, a survey ensues of the advantages and drawbacks of the quinones commonly used in Complex I activity determination and of their kinetic properties. The available evidence is then displayed on structure-activity relationships of various quinone compounds in terms of electron transfer activity and proton translocation, and the present knowledge is discussed in terms of the nature of multiple quinone-binding sites in the Complex.
Lenaz
G
G
Dipartimento di Biochimica 'G. Moruzzi', University of Bologna, Via Irnerio 48, 40126 Bologna, Italy. lenaz@biocfarm.unibo.it
D016660:NAD(P)H Dehydrogenase (Quinone) / Q000737:chemistry* / Q000378:metabolism; D011809:Quinones / Q000737:chemistry*; D013329:Structure-Activity Relationship
D011809:Quinones; D016660:NAD(P)H Dehydrogenase (Quinone)