The arrangement and function of the redox centers of the mammalian bc1 complex is described on the basis of structural data derived from amino acid sequence studies and secondary structure predictions and on the basis of functional studies (i.e., EPR data, inhibitor studies, and kinetic experiments). Two ubiquinone reaction centers do exist--a QH2 oxidation center situated at the outer, cytosolic surface of the cristae membrane (Q0 center), and a Q reduction center (Qi center) situated more to the inner surface of the cristae membrane. The Q0 center is formed by the b-566 domain of cytochrome b, the FeS protein, and maybe an additional small subunit, whereas the Qi center is formed by the b-562 domain of cytochrome b and presumably the 13.4 kDa protein ("QP-C"). The "Q binding proteins" are proposed to be protein subunits of the Q reaction centers of various multiprotein complexes. The path of electron flow branches at the Q0 center, half of the electrons flowing via the high-potential cytochrome chain to oxygen and half of the electrons cycling back into the Q pool via the cytochrome b path connecting the two Q reaction centers. During oxidation of QH2, 2H+ are released to the cytosolic space and during reduction of Q, 2H+ are taken up from the matrix side, resulting in a net transport across the membrane of 2H+ per e- flown from QH2 to cytochrome c, the H+ being transported across the membrane as H (H+ + e-) by the mobile carrier Q. The authors correct their earlier view of cytochrome b functioning as a H+ pump, proposing that the redox-linked pK changes of the acidic groups of cytochrome b are involved in the protonation/deprotonation processes taking place during the reduction and oxidation of Q. The reviewers stress that cytochrome b is in equilibrium with the Q pool via the Qi center, but not via the Q0 center. Their view of the mechanisms taking place at the reductase is a Q cycle linked to a Q-pool where cytochrome b is acting as an electron pump.