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10.1074/jbc.M115.711770 http://scihub22266oqcxt.onion/10.1074/jbc.M115.711770 C5104913!5104913 !27605664     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 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\27605664 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Biol+Chem 2016 ; 291 (46 ): 23882-23894 Nephropedia Template TP {{tp|p=27605664 |t=2016. The Mg2+-containing Water Cluster of Mammalian Cytochrome c Oxidase Collects Four Pumping Proton Equivalents in Each Catalytic Cycle |pdf=|usr=}}{{27605664 }} gab.com Text The Mg2+-containing Water Cluster of Mammalian Cytochrome c Oxidase Collects Four Pumping Proton Equivalents in Each Catalytic Cycle JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=27605664 #FOAvip Bovine heart cytochrome c oxidase (CcO) pumps four proton equivalents per catalytic cycle through the H-pathway, a proton-conducting pathway, which includes a hydrogen bond network and a water channel operating in tandem. Protons are transferred by H(3)O(+) through the water channel from the N-side into the hydrogen bond network, where they are pumped to the P-side by electrostatic repulsion between protons and net positive charges created at heme a as a result of electron donation to O(2) bound to heme a(3) To block backward proton movement, the water channel remains closed after O(2) binding until the sequential four-proton pumping process is complete. Thus, the hydrogen bond network must collect four proton equivalents before O(2) binding. However, a region with the capacity to accept four proton equivalents was not discernable in the x-ray structures of the hydrogen bond network. The present x-ray structures of oxidized/reduced bovine CcO are improved from 1.8/1.9 to 1.5/1.6 Å resolution, increasing the structural information by 1.7/1.6 times and revealing that a large water cluster, which includes a Mg(2+) ion, is linked to the H-pathway. The cluster contains enough proton acceptor groups to retain four proton equivalents. The redox-coupled x-ray structural changes in Glu(198), which bridges the Mg(2+) and Cu(A) (the initial electron acceptor from cytochrome c) sites, suggest that the Cu(A)-Glu(198)-Mg(2+) system drives redox-coupled transfer of protons pooled in the water cluster to the H-pathway. Thus, these x-ray structures indicate that the Mg(2+)-containing water cluster is the crucial structural element providing the effective proton pumping in bovine CcO. Twit Text FOAVip The Mg2+-containing Water Cluster of Mammalian Cytochrome c Oxidase Collects Four Pumping Proton Equivalents in Each Catalytic Cycle ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=27605664 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27605664 #FOAvip English Wikipedia <ref>{{Cite pmid|27605664 }}</ref> The Mg2+-containing Water Cluster of Mammalian Cytochrome c Oxidase Collects Four Pumping Proton Equivalents in Each Catalytic Cycle #MMPMID27605664 Yano N ; Muramoto K ; Shimada A ; Takemura S ; Baba J ; Fujisawa H ; Mochizuki M ; Shinzawa-Itoh K ; Yamashita E ; Tsukihara T ; Yoshikawa S J Biol Chem 2016[Nov]; 291 (46 ): 23882-23894 PMID27605664 show ga Bovine heart cytochrome c oxidase (CcO) pumps four proton equivalents per catalytic cycle through the H-pathway, a proton-conducting pathway, which includes a hydrogen bond network and a water channel operating in tandem. Protons are transferred by H(3)O(+) through the water channel from the N-side into the hydrogen bond network, where they are pumped to the P-side by electrostatic repulsion between protons and net positive charges created at heme a as a result of electron donation to O(2) bound to heme a(3) To block backward proton movement, the water channel remains closed after O(2) binding until the sequential four-proton pumping process is complete. Thus, the hydrogen bond network must collect four proton equivalents before O(2) binding. However, a region with the capacity to accept four proton equivalents was not discernable in the x-ray structures of the hydrogen bond network. The present x-ray structures of oxidized/reduced bovine CcO are improved from 1.8/1.9 to 1.5/1.6 Å resolution, increasing the structural information by 1.7/1.6 times and revealing that a large water cluster, which includes a Mg(2+) ion, is linked to the H-pathway. The cluster contains enough proton acceptor groups to retain four proton equivalents. The redox-coupled x-ray structural changes in Glu(198), which bridges the Mg(2+) and Cu(A) (the initial electron acceptor from cytochrome c) sites, suggest that the Cu(A)-Glu(198)-Mg(2+) system drives redox-coupled transfer of protons pooled in the water cluster to the H-pathway. Thus, these x-ray structures indicate that the Mg(2+)-containing water cluster is the crucial structural element providing the effective proton pumping in bovine CcO. |*Models, Molecular [MESH] |Animals [MESH] |Cattle [MESH] |Crystallography, X-Ray [MESH] |Electron Transport Complex IV/*chemistry/metabolism [MESH] |Magnesium/*chemistry/metabolism [MESH] |Protein Structure, Quaternary [MESH] |Proton Pumps/*chemistry/metabolism [MESH]The Mg2+-containing Water Cluster of Mammalian Cytochrome c Oxidase Co(epmc).pdf DeepDyve Pubget Overpricing