Abstract：
:Mitochondrial cytochrome oxidase is a functionally complex, membrane-bound respiratory enzyme which catalyses both the reduction of O2 to water and proton-pumping. During respiration, an exogenous donor, cytochrome c, donates four electrons to O2 bound at the bimetallic haem alpha 3 Fe-Cu centre within the enzyme. These four electron transfers are mediated by the enzyme's haem alpha and CuA redox centres and result in the translocation of four protons across the inner mitochondrial membrane. The molecular mechanism of proton translocation has not yet been delineated, however, and in the absence of direct experimental evidence all four electron transfers have been assumed to couple equally to proton-pumping. Here, I report the effects of proton-motive force and membrane potential on two equilibria involving intermediates of the bimetallic centre at different levels of O2 reduction. The results show that only two of the electron transfers, to the 'peroxy' and 'oxyferryl' intermediates of the bimetallic centre, are linked to proton translocation, a finding which strongly constrains candidate mechanisms for proton-pumping.
journal_name
Naturejournal_title
Natureauthors
Wikström Mdoi
10.1038/338776a0subject
Has Abstractpub_date
1989-04-27 00:00:00pages
776-8issue
6218eissn
0028-0836issn
1476-4687journal_volume
338pub_type
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