Triphasic reduction of bH and the absence of equilibration at the i-site of bc1 complex.
The concept of a stabilized semiquinone radical forming the basis of a two-electron gate has long been familiar in the context of the quinone-reducing site in photosynthetic systems and has already been suggested to play a role at the i-site of the bc1-type complexes. It is here pointed out that this concept is sufficient to explain the so-called triphasic reduction kinetics of cytochrome bH, in which cytochrome bH goes partially reduced, is reoxidized and then goes fully reduced. The rate constants for binding and unbinding of quinone, quinol and semiquinone at the i-site are discussed, and a kinetic model featuring slow release of the i-site semiquinone is shown to display many features of the kinetics of electron transfer at the i-site.
West
I C
IC
Glynn Research Institute, Bodmin, U.K.
D014450:Electron Transport Complex III / Q000378:metabolism*; D007700:Kinetics; D008433:Mathematics; D008962:Models, Theoretical; D010084:Oxidation-Reduction; D013816:Thermodynamics
D014450:Electron Transport Complex III