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10.1038/srep12047 http://scihub22266oqcxt.onion/10.1038/srep12047 C4550891!4550891!26310633     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       Sci+Rep 2015 ; 5 (ä): ä Nephropedia Template TP {{tp|p=26310633|t=2015. Structural Changes and Proton Transfer in Cytochrome c Oxidase |pdf=|usr=}}{{26310633}} gab.com Text Structural Changes and Proton Transfer in Cytochrome c Oxidase JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26310633 #FOAvip In cytochrome c oxidase electron transfer from cytochrome c to O2 is linked to transmembrane proton pumping, which contributes to maintaining a proton electrochemical gradient across the membrane. The mechanism by which cytochrome c oxidase couples the exergonic electron transfer to the endergonic proton translocation is not known, but it presumably involves local structural changes that control the alternating proton access to the two sides of the membrane. Such redox-induced structural changes have been observed in X-ray crystallographic studies at residues 423?425 (in the R. sphaeroides oxidase), located near heme a. The aim of the present study is to investigate the functional effects of these structural changes on reaction steps associated with proton pumping. Residue Ser425 was modified using site-directed mutagenesis and time-resolved spectroscopy was used to investigate coupled electron-proton transfer upon reaction of the oxidase with O2. The data indicate that the structural change at position 425 propagates to the D proton pathway, which suggests a link between redox changes at heme a and modulation of intramolecular proton-transfer rates. Twit Text FOAVip Structural Changes and Proton Transfer in Cytochrome c Oxidase ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26310633 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26310633 #FOAvip English Wikipedia <ref>{{Cite pmid|26310633}}</ref> Structural Changes and Proton Transfer in Cytochrome c Oxidase #MMPMID26310633 Vilhjálmsdóttir J; Johansson AL; Brzezinski P Sci Rep 2015[]; 5 (ä): ä PMID26310633show ga In cytochrome c oxidase electron transfer from cytochrome c to O2 is linked to transmembrane proton pumping, which contributes to maintaining a proton electrochemical gradient across the membrane. The mechanism by which cytochrome c oxidase couples the exergonic electron transfer to the endergonic proton translocation is not known, but it presumably involves local structural changes that control the alternating proton access to the two sides of the membrane. Such redox-induced structural changes have been observed in X-ray crystallographic studies at residues 423?425 (in the R. sphaeroides oxidase), located near heme a. The aim of the present study is to investigate the functional effects of these structural changes on reaction steps associated with proton pumping. Residue Ser425 was modified using site-directed mutagenesis and time-resolved spectroscopy was used to investigate coupled electron-proton transfer upon reaction of the oxidase with O2. The data indicate that the structural change at position 425 propagates to the D proton pathway, which suggests a link between redox changes at heme a and modulation of intramolecular proton-transfer rates. äStructural Changes and Proton Transfer in Cytochrome c Oxidase (epmc).pdf DeepDyve Pubget Overpricing