Operation of the modified Q cycle in Complex III results in the reduction of Cytochrome c, oxidation of ubiquinol to ubiquinone, and the transfer of four protons into the intermembrane space, per two-cycle process.
Ubiquinol (QH) binds to the Q site of complex III via hydrogen bonding to His182 of the Rieske iron-sulfur protein and Glu272 of Cytochrome b. Ubiquinone (Q), in turn, binds the Q site of complex III.  Ubiquinol is divergently oxidized (gives up one electron each) to the Rieske iron-sulfur (FeS) protein and to the b heme.  This oxidation reaction produces a transient semiquinone before complete oxidation to ubiquinone, which then leaves the Q site of complex III.
Having acquired one electron from ubiquinol, the FeS protein is freed from its electron donor and is able to migrate to the Cytochrome c subunit. FeS protein then donates its electron to Cytochrome c, reducing its bound heme group. The electron is from there transferred to an oxidized molecule of Cytochrome c externally bound to complex III, which then dissociates from the complex.  In addition, the reoxidation of the FeS protein releases the proton bound to His181 into the intermembrane space.
The other electron, which was transferred to the b heme, is used to reduce the b heme, which in turn transfers the electron to the ubiquinone bound at the Q site. The movement of this electron is energetically unfavourable, as the electron is moving towards the negatively charged side of the membrane. This is offset by a favourable change in E from −100 mV in B to +50mV in the B heme.  The attached ubiquinone is thus reduced to a semiquinone radical. The proton taken up by Glu272 is subsequently transferred to a hydrogen-bonded water chain as Glu272 rotates 170° to hydrogen bond a water molecule, in turn hydrogen-bonded to a propionate of the b heme.
Because the last step leaves an unstable semiquinone at the Q site, the reaction is not yet fully completed.  A second Q cycle is necessary, with the second electron transfer from cytochrome b reducing the semiquinone to ubiquinol. The ultimate products of the Q cycle are four protons entering the intermembrane space, two from the matrix and two from the reduction of two molecules of cytochrome c.  The reduced cytochrome c is eventually reoxidized by complex IV. The process is cyclic as the ubiquinol created at the Q site can be reused by binding to the Q site of complex III.