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10.1016/j.bbabio.2018.03.016 http://scihub22266oqcxt.onion/10.1016/j.bbabio.2018.03.016 C5955396!5955396 !29625088     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29625088 &cmd=llinks): Failed to open stream: HTTP request failed! 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Dissecting the pattern of proton release from partial process involved in ubihydroquinone oxidation in the Q-cycle |pdf=|usr=}}{{29625088 }} gab.com Text Dissecting the pattern of proton release from partial process involved in ubihydroquinone oxidation in the Q-cycle JO: Biochim Biophys Acta Bioenerg http://www.kidney.de/pget.php?&tw=1&pmid=29625088 #FOAvip A key feature of the modified Q-cycle of the cytochrome bc(1) and related complexes is a bifurcation of QH(2) oxidation involving electron transfer to two different acceptor chains, each coupled to proton release. We have studied the kinetics of proton release in chromatophore vesicles from Rhodobacter sphaeroides, using the pH-sensitive dye neutral red to follow pH changes inside on activation of the photosynthetic chain, focusing on the bifurcated reaction, in which 4H(+)are released on complete turnover of the Q-cycle (2H(+)/ubiquinol (QH(2)) oxidized). We identified different partial processes of the Q(o)-site reaction, isolated through use of specific inhibitors, and correlated proton release with electron transfer processes by spectrophotometric measurement of cytochromes or electrochromic response. In the presence of myxothiazol or azoxystrobin, the proton release observed reflected oxidation of the Rieske iron?sulfur protein. In the absence of Q(o)-site inhibitors, the pH change measured represented the convolution of this proton release with release of protons on turnover of the Q(o)-site, involving formation of the ES-complex and oxidation of the semiquinone intermediate. Turnover also regenerated the reduced iron-sulfur protein, available for further oxidation on a second turnover. Proton release was well-matched with the rate limiting step on oxidation of QH(2) on both turnovers. However, a minor lag in proton release found at pH?7 but not at pH?8 might suggest that a process linked to rapid proton release on oxidation of the intermediate semiquinone involves a group with a pK in that range. Twit Text FOAVip Dissecting the pattern of proton release from partial process involved in ubihydroquinone oxidation in the Q-cycle ????Biochim Biophys Acta Bioenerg http://www.kidney.de/pget.php?&tw=1&pmid=29625088 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29625088 #FOAvip English Wikipedia <ref>{{Cite pmid|29625088 }}</ref> Dissecting the pattern of proton release from partial process involved in ubihydroquinone oxidation in the Q-cycle #MMPMID29625088 Wilson CA ; Crofts AR Biochim Biophys Acta Bioenerg 2018[Jul]; 1859 (7 ): 531-543 PMID29625088 show ga A key feature of the modified Q-cycle of the cytochrome bc(1) and related complexes is a bifurcation of QH(2) oxidation involving electron transfer to two different acceptor chains, each coupled to proton release. We have studied the kinetics of proton release in chromatophore vesicles from Rhodobacter sphaeroides, using the pH-sensitive dye neutral red to follow pH changes inside on activation of the photosynthetic chain, focusing on the bifurcated reaction, in which 4H(+)are released on complete turnover of the Q-cycle (2H(+)/ubiquinol (QH(2)) oxidized). We identified different partial processes of the Q(o)-site reaction, isolated through use of specific inhibitors, and correlated proton release with electron transfer processes by spectrophotometric measurement of cytochromes or electrochromic response. In the presence of myxothiazol or azoxystrobin, the proton release observed reflected oxidation of the Rieske iron?sulfur protein. In the absence of Q(o)-site inhibitors, the pH change measured represented the convolution of this proton release with release of protons on turnover of the Q(o)-site, involving formation of the ES-complex and oxidation of the semiquinone intermediate. Turnover also regenerated the reduced iron-sulfur protein, available for further oxidation on a second turnover. Proton release was well-matched with the rate limiting step on oxidation of QH(2) on both turnovers. However, a minor lag in proton release found at pH?7 but not at pH?8 might suggest that a process linked to rapid proton release on oxidation of the intermediate semiquinone involves a group with a pK in that range. |*Protons [MESH] |Antimycin A/analogs & derivatives/pharmacology [MESH] |Electron Transport [MESH] |Electron Transport Complex III/*chemistry [MESH] |Hydrogen-Ion Concentration [MESH] |Methacrylates/pharmacology [MESH] |Oxidation-Reduction [MESH] |Polyenes/pharmacology [MESH] |Rhodobacter sphaeroides/metabolism [MESH]Dissecting the pattern of proton release from partial process involved(epmc).pdf DeepDyve Pubget Overpricing