Abstract:
:The cytochrome bc(1) complex catalyzes electron transfer from ubiquinol to cytochrome c by a protonmotive Q cycle mechanism in which electron transfer is linked to proton translocation across the inner mitochondrial membrane. In the Q cycle mechanism proton translocation is the net result of topographically segregated reduction of quinone and reoxidation of quinol on opposite sides of the membrane, with protons being carried across the membrane as hydrogens on the quinol. The linkage of proton chemistry to electron transfer during quinol oxidation and quinone reduction requires pathways for moving protons to and from the aqueous phase and the hydrophobic environment in which the quinol and quinone redox reactions occur. Crystal structures of the mitochondrial cytochrome bc(1) complexes in various conformations allow insight into possible proton conduction pathways. In this review we discuss pathways for proton conduction linked to ubiquinone redox reactions with particular reference to recently determined structures of the yeast bc(1) complex.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Hunte C,Palsdottir H,Trumpower BLdoi
10.1016/s0014-5793(03)00391-0keywords:
subject
Has Abstractpub_date
2003-06-12 00:00:00pages
39-46issue
1eissn
0014-5793issn
1873-3468pii
S0014579303003910journal_volume
545pub_type
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