Sandbox Reserved 1600: Difference between revisions
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==Electron Source== | ==Electron Source== | ||
An electron source is needed in order for the redox reaction of O₂ to occur. Cytochrome bd oxidase uses the quinol molecule ubiquinone as an electron donor. The chemical structure of ubiquinone is shown in Fig. 2. [[Image:Ubiquinone.jpg|200 px|right|thumb|Figure 2. Chemical structure of ubiquinone.]] As shown in the <scene name='83/838655/Bdoxidase_structure_full/4'>overall structure</scene> the <scene name='83/838655/Bdoxidase_q_loop/2'>Q loop</scene> is on the extracellular surface and provides a binding site for ubiquinone. <ref name = ”Safarian” /> As mentioned in the Active Site section, Heme <scene name='83/838655/Bdoxidase_qloop_zoom/3'>B558</scene> is closest in proximity to the Q loop and thus is the suggested electron acceptor. This suggestion is further supported by the conservation of <scene name='83/838655/ | An electron source is needed in order for the redox reaction of O₂ to occur. Cytochrome bd oxidase uses the quinol molecule ubiquinone as an electron donor. The chemical structure of ubiquinone is shown in Fig. 2. [[Image:Ubiquinone.jpg|200 px|right|thumb|Figure 2. Chemical structure of ubiquinone.]] As shown in the <scene name='83/838655/Bdoxidase_structure_full/4'>overall structure</scene> the <scene name='83/838655/Bdoxidase_q_loop/2'>Q loop</scene> is on the extracellular surface and provides a binding site for ubiquinone. <ref name = ”Safarian” /> As mentioned in the Active Site section, Heme <scene name='83/838655/Bdoxidase_qloop_zoom/3'>B558</scene> is closest in proximity to the Q loop and thus is the suggested electron acceptor. This suggestion is further supported by the conservation of <scene name='83/838655/Bdoxidase_trp/1'>Trp374</scene> often found as intermediate electron receptors in biological electron transfer chains. <ref name =”Safarian” /> | ||
==Potential Proton Pathways== | ==Potential Proton Pathways== | ||