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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 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\28265060 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Proc+Natl+Acad+Sci+U+S+A 2017 ; 114 (11 ): 2916-2921 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 In MtrF, an outer-membrane multiheme cytochrome, the 10 heme groups are arranged in heme binding domains II and IV along the pseudo-C(2) axis, forming the electron transfer (ET) pathways. Previous reports based on molecular dynamics simulations showed that the redox potential (E(m)) values for the heme pairs located in symmetrical positions in domains II and IV were similar, forming bidirectional ET pathways [Breuer M, Zarzycki P, Blumberger J, Rosso KM (2012) J Am Chem Soc 134(24):9868-9871]. Here, we present the E(m) values of the 10 hemes in MtrF, solving the linear Poisson-Boltzmann equation and considering the protonation states of all titratable residues and heme propionic groups. In contrast to previous studies, the E(m) values indicated that the ET is more likely to be downhill from domain IV to II because of localization of acidic residues in domain IV. Reduction of hemes in MtrF lowered the E(m) values, resulting in switching to alternative downhill ET pathways that extended to the flavin binding sites. These findings present an explanation of how MtrF serves as an electron donor to extracellular substrates. 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 ): 2916-2921 PMID28265060 show ga In MtrF, an outer-membrane multiheme cytochrome, the 10 heme groups are arranged in heme binding domains II and IV along the pseudo-C(2) axis, forming the electron transfer (ET) pathways. Previous reports based on molecular dynamics simulations showed that the redox potential (E(m)) values for the heme pairs located in symmetrical positions in domains II and IV were similar, forming bidirectional ET pathways [Breuer M, Zarzycki P, Blumberger J, Rosso KM (2012) J Am Chem Soc 134(24):9868-9871]. Here, we present the E(m) values of the 10 hemes in MtrF, solving the linear Poisson-Boltzmann equation and considering the protonation states of all titratable residues and heme propionic groups. In contrast to previous studies, the E(m) values indicated that the ET is more likely to be downhill from domain IV to II because of localization of acidic residues in domain IV. Reduction of hemes in MtrF lowered the E(m) values, resulting in switching to alternative downhill ET pathways that extended to the flavin binding sites. These findings present an explanation of how MtrF serves as an electron donor to extracellular substrates. |*Electron Transport [MESH] |Amino Acid Sequence [MESH] |Binding Sites [MESH] |Heme/chemistry/metabolism [MESH] |Hydrogen Bonding [MESH] |Ligands [MESH] |Mitochondrial Proteins/chemistry/*metabolism [MESH] |Models, Molecular [MESH] |Protein Binding [MESH] |Protein Conformation [MESH] |Protein Interaction Domains and Motifs [MESH]Electron transfer pathways in a multiheme cytochrome MtrF (epmc).pdf DeepDyve Pubget Overpricing