Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1073/pnas.1617615114 http://scihub22266oqcxt.onion/10.1073/pnas.1617615114 C5358398!5358398!28265060     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       Proc+Natl+Acad+Sci+U+S+A 2017 ; 114 (11): 2916-21 Nephropedia Template TP {{tp|p=28265060|t=2017. Electron transfer pathways in a multiheme cytochrome MtrF |pdf=|usr=}}{{28265060}} gab.com Text Electron transfer pathways in a multiheme cytochrome MtrF JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28265060 #FOAvip Cellular respiration process in dissimilatory metal-reducing bacteria is coupled to electron transfer. In Shewanella species, a decaheme cytochrome MtrF transfers electrons to extracellular insoluble substrates, such as Fe(III) and Mn(III/IV). Using the atomic coordinates of the MtrF crystal structure and analyzing interactions with the protein environments, we calculated the redox potential (Em) values of the 10 hemes in MtrF. The Em profiles show how the electron transfer pathways proceed in MtrF. We showed that, when MtrF is reduced, the direction of the ET pathway switches, and bound flavin becomes the terminal electron acceptor. Twit Text FOAVip Electron transfer pathways in a multiheme cytochrome MtrF ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28265060 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28265060 #FOAvip English Wikipedia <ref>{{Cite pmid|28265060}}</ref> Electron transfer pathways in a multiheme cytochrome MtrF #MMPMID28265060 Watanabe HC; Yamashita Y; Ishikita H Proc Natl Acad Sci U S A 2017[Mar]; 114 (11): 2916-21 PMID28265060show ga Cellular respiration process in dissimilatory metal-reducing bacteria is coupled to electron transfer. In Shewanella species, a decaheme cytochrome MtrF transfers electrons to extracellular insoluble substrates, such as Fe(III) and Mn(III/IV). Using the atomic coordinates of the MtrF crystal structure and analyzing interactions with the protein environments, we calculated the redox potential (Em) values of the 10 hemes in MtrF. The Em profiles show how the electron transfer pathways proceed in MtrF. We showed that, when MtrF is reduced, the direction of the ET pathway switches, and bound flavin becomes the terminal electron acceptor. äElectron transfer pathways in a multiheme cytochrome MtrF (epmc).pdf DeepDyve Pubget Overpricing