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- W2478677615 endingPage "434" @default.
- W2478677615 startingPage "419" @default.
- W2478677615 abstract "The cytochrome bc 1 complex of eukaryotic mitochondrial and prokaryotic energy transducing membranes functions as a protonmotive quinol:cytochrome c oxidoreductase. The enzyme utilizes a highly characteristic ‘Q-cycle’ reaction mechanism in which oxidation of substrate quinol leads to a bifurcated electron transfer pathway. This mechanism generates a highly-reducing, reactive radical semiquinone (SQo) intermediate at the site of quinol oxidation (Qo) within cytochrome b which must be tightly managed to prevent energetically wasteful electron transfer side reactions or reduction of dioxygen to biologically harmful superoxide. In this chapter we discuss mechanistic strategies harnessed by the bc 1 complex to minimize unproductive electron transfer from SQo with particular reference to superoxide generation. Recent work suggests that the bc 1 complex achieves this by kinetically trapping the SQo anion within a hydrophobic region of the Qo pocket as a destabilized, low-occupancy intermediate, conserving redox energy to reduce the native electron acceptor (ferriheme b L) while minimizing the probability of unwanted (and potentially damaging) electron transfer bypass reactions." @default.
- W2478677615 created "2016-08-23" @default.
- W2478677615 creator A5021772801 @default.
- W2478677615 creator A5026479447 @default.
- W2478677615 creator A5079248597 @default.
- W2478677615 date "2016-01-01" @default.
- W2478677615 modified "2023-09-26" @default.
- W2478677615 title "Electron Transfer Reactions at the Qo Site of the Cytochrome bc 1 Complex: The Good, the Bad, and the Ugly" @default.
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- W2478677615 doi "https://doi.org/10.1007/978-94-017-7481-9_21" @default.
- W2478677615 hasPublicationYear "2016" @default.
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