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. Author manuscript; available in PMC: 2018 Jul 1.
Published in final edited form as: Biochim Biophys Acta. 2018 Apr 3;1859(7):531–543. doi: 10.1016/j.bbabio.2018.03.016

Fig. 1.

Fig. 1

Q-cycle scheme. A monomer of the bc1 complex is shown with the Qo-site in the ES-complex configuration, and with antimycin bound at the Qi-site (in the uninhibited complex, the Qi-site would be occupied by a quinone). In the ES-complex, QH2 is bound to oxidized ISPox; H152 of the ISP-subunit ligands Fe2 of the 2Fe2S cluster (shown as space-filling spheres), and H-bonds to QH2. Redox centers are highlighted as stick models, with QH2 in orange, antimycin in yellow, and others in CPK colors, and residues in the cyt b-subunit of importance in proton exit (E295, Y147, N279, R94, see text for discussion) are similarly shown.