7.1.1.8 additional information activity of enzyme complex III of the mitochondrial electron transport chain is essential for early heart muscle cell differentiation 7.1.1.8 additional information enzyme complex III is part of the mitochondrial membrane electron transport chain 7.1.1.8 additional information enzyme is a central component of cellular energy conservation machinery 7.1.1.8 additional information enzyme is part of the Knallgas reaction pathway 7.1.1.8 additional information the Qo-cycle, overview 7.1.1.8 additional information the enzyme is a component of the multienzyme complex III 7.1.1.8 additional information the physiological impact of a mixed Q pool in RQ-producing organisms, overview 7.1.1.8 additional information photosynthetic growth of purple non-sulfur bacteria such as Rhodobacter capsulatus depends on the cyclic electron transfer between the ubihydroquinone:cytochrome c oxidoreductases (cyt bc1 complex), and the photochemical reaction centers, mediated by either a membrane-bound or a freely diffusible electron carrier 7.1.1.8 additional information reaction mechanism of superoxide generation by bc1, overview 7.1.1.8 additional information reaction mechanism of superoxide generation by bc1, overview. Maximum superoxide anions generation activity is observed when the complex is inhibited by antimycin A or inactivated by heat treatment or proteinase K digestion. The protein subunits, at least those surrounding the QP pocket, may play a role either in preventing the release of superoxide. from its production site to aqueous environments or in preventing O2 from getting access to the hydrophobic QP pocket and might not directly participate in superoxide production 7.1.1.8 naphthoquinol + 2 ferricytochrome c - 7.1.1.8 quinol + 2 ferricytochrome c - 7.1.1.8 ubiquinol + 2 ferricytochrome c - 7.1.1.8 ubiquinol + 2 ferricytochrome c the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced 7.1.1.8 ubiquinol + 2 ferricytochrome c the cyt bc1 complex catalyzes the antimycin-sensitive electron transfer reaction from lipophilic substrate ubiquinol to cytochrome c coupled with proton translocation across the membrane. As a result, for every quinol molecule oxidized, four protons are deposited to the positive side of the membrane and two molecules of cytochrome c are reduced. Key step in the Q-cycle mechanism is the separation of the two electrons of the substrate quinol at the QP site 7.1.1.8 ubiquinol + 2 ferricytochrome c552 - 7.1.1.8 ubiquinol + ferricytochrome c - 7.1.1.8 ubiquinol + ferricytochrome c the cytochrome bc1 complex resides in the inner membrane of mitochondria and transfers electrons from ubiquinol to cytochrome c, this electron transfer is coupled to the translocation of protons across the membrane by the protonmotive Q cycle mechanism, this mechanism topographically separates reduction of quinone and reoxidation of quinol at sites on opposite sites of the membrane, referred to as center N, Qn site, and center P, Qp site, respectively 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c - 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c electron transfer between yeast cytochrome bc1 complex and cytochrome c is coupled to proton transport across the inner mitochondrial membrane delivering a membrane potential, enzyme complex is important in cell respiration and photosynthesis 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c enzyme catalyzes the electron transfer from a quinol molecule to cytochrome c, and concomitantly translocates protons across membranes for ATP synthesis and various cellular processes 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c enzyme complex is essentially involved in the mitochondrial respiratory electron transfer chain 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation 7.1.1.8 ubiquinol-2 + 2 ferricytochrome c ubiquinol oxidation is part of the protonmotive Q cycle mechanism, overview, half-of-the sites mechanism with reciprocal control between high potential and low potential redox components involved in ubiquinol oxidation 7.1.1.8 ubiquinol-2 + ferricytochrome c the cytochrome bc1 complex is the central segment of the respiratory chain in mitochondria 7.1.1.8 ubiquinone-10 + ferricytochrome c -