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10.1038/s41598-018-25779-w http://scihub22266oqcxt.onion/10.1038/s41598-018-25779-w C5951807!5951807!29760451     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\29760451.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Sci+Rep 2018 ; 8 (ä): ä Nephropedia Template TP {{tp|p=29760451|t=2018. The electron distribution in the ?activated? state of cytochrome c oxidase |pdf=|usr=}}{{29760451}} gab.com Text The electron distribution in the activated state of cytochrome c oxidase JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=29760451 #FOAvip Cytochrome c oxidase catalyzes reduction of O2 to H2O at a catalytic site that is composed of a copper ion and heme group. The reaction is linked to translocation of four protons across the membrane for each O2 reduced to water. The free energy associated with electron transfer to the catalytic site is unequal for the four electron-transfer events. Most notably, the free energy associated with reduction of the catalytic site in the oxidized cytochrome c oxidase (state O) is not sufficient for proton pumping across the energized membrane. Yet, this electron transfer is mechanistically linked to proton pumping. To resolve this apparent discrepancy, a high-energy oxidized state (denoted OH) was postulated and suggested to be populated only during catalytic turnover. The difference between states O and OH was suggested to be manifested in an elevated midpoint potential of CuB in the latter. This proposal predicts that one-electron reduction of cytochrome c oxidase after its oxidation would yield re-reduction of essentially only CuB. Here, we investigated this process and found ~5% and ~6% reduction of heme a3 and CuB, respectively, i.e. the apparent redox potentials for heme a3 and CuB are lower than that of heme a. Twit Text FOAVip The electron distribution in the activated state of cytochrome c oxidase ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=29760451 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29760451 #FOAvip English Wikipedia <ref>{{Cite pmid|29760451}}</ref> The electron distribution in the ?activated? state of cytochrome c oxidase #MMPMID29760451 Vilhjálmsdóttir J; Gennis RB; Brzezinski P Sci Rep 2018[]; 8 (ä): ä PMID29760451show ga Cytochrome c oxidase catalyzes reduction of O2 to H2O at a catalytic site that is composed of a copper ion and heme group. The reaction is linked to translocation of four protons across the membrane for each O2 reduced to water. The free energy associated with electron transfer to the catalytic site is unequal for the four electron-transfer events. Most notably, the free energy associated with reduction of the catalytic site in the oxidized cytochrome c oxidase (state O) is not sufficient for proton pumping across the energized membrane. Yet, this electron transfer is mechanistically linked to proton pumping. To resolve this apparent discrepancy, a high-energy oxidized state (denoted OH) was postulated and suggested to be populated only during catalytic turnover. The difference between states O and OH was suggested to be manifested in an elevated midpoint potential of CuB in the latter. This proposal predicts that one-electron reduction of cytochrome c oxidase after its oxidation would yield re-reduction of essentially only CuB. Here, we investigated this process and found ~5% and ~6% reduction of heme a3 and CuB, respectively, i.e. the apparent redox potentials for heme a3 and CuB are lower than that of heme a. äThe electron distribution in the ?activated? state of cytochrome c oxi(epmc).pdf DeepDyve Pubget Overpricing