作者: Romana Fato , Ernesto Estornell , Salvatore Di Bernardo , Francesco Pallotti , Giovanna Parenti Castelli
DOI: 10.1021/BI9516034
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摘要: The reduction kinetics of coenzyme Q (CoQ, ubiquinone) by NADH:ubiquinone oxidoreductase (complex I, EC 1.6.99.3) was investigated in bovine heart mitochondrial membranes using water-soluble homologs and analogs the endogenous ubiquinone acceptor CoQ10 [the lower from CoQ0 to CoQ3, 6-pentyl (PB) 6-decyl (DB) analogs, duroquinone]. By far best substrates submitochondrial particles are CoQ1 PB. NADH−CoQ reductase detail PB as acceptors. kinetic pattern follows a ping-pong mechanism; Km for is range 20 μM but reversibly increased 60 extraction CoQ10. CoQ10-depleted indicates that not only does exert significant product inhibition rather required appropriate structure site. much Vmax with CoQ2 DB acceptor, associated an almost identical Km, sug...