The coenzyme Q—cytochrome c reductase complex, sometimes called the cytochrome bc1 complex, and at other times complex III, is the third complex in the electron transport chain (, ). It is a transmembrane lipoprotein, and it catalyzes the reduction of cytochrome c by accepting reducing equivalents from coenzyme Q (CoQ):
- QH2 + 2 Fe+3—cytochrome c + 2 H+in → Q + 2 Fe+2—cytochrome c + 4 H+out
In the process called Q cycle, two protons are consumed from the matrix, four protons are released into the inter membrane space and two electrons are passed to cytochrome c.
Structure
Compared to the other major proton pumping subunits of the
electron transport chain, the number of subunits found can be small, as small as three polypeptide chains. This number does increase, and as many as eleven subunits can be found in higher animals. The
prosthetic groups in the complex are a pair of
heme b (
bL and
bH), one heme
c (
c1), and a two iron, two sulfur
iron-sulfur cluster (2Fe•2S).
Inhibitors of complex III
Antimycin A binds to the Q
i site and inhibits the transfer of electrons in Complex III from heme
bH to oxidized Q.
Myxothiazol and
Stigmatellin binds to the Q
o site und inhibits the transfer of electrons from reduced QH
2 to cytochrome
c.
Some have been commercialized as fungicides (the strobilurin derivates) and as anti-malaria agents (atovaquone).
Oxygen free radicals
A small fraction of electrons leave the electron tranport chain before reaching complex IV. Premature electron leakage to oxygen results in the formation of
superoxide. The relevance of this otheriwse minor side reaction is that superoxide and other reactive oxygen species are thought to play a role in several pathologies, including aging. Electron leakage occurs mainly at the Q
o site and is stimulated by antimycin A. Antimycin A locks the
b hemes in the reduced state by preventing their re-oxidation at the Q
i site, which in turn causes the steady state concentrations of the Q
o semiquinone to rise, the latter species reacting with oxygen to form superoxide. The effect of high membrane potential is thought to have a similar effect.
See also
External links
Cellular respiration | EC 1.10.2 | Iron-sulfur proteins
Cytochrom c Reduktase