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10.3389/fchem.2017.00017 http://scihub22266oqcxt.onion/10.3389/fchem.2017.00017 C5352715!5352715!28361051     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Front+Chem 2017 ; 5 (ä): ä Nephropedia Template TP {{tp|p=28361051|t=2017. On the Role of Additional 4Fe-4S Clusters with a Free Coordination Site in Radical-SAM Enzymes |pdf=|usr=}}{{28361051}} gab.com Text On the Role of Additional 4Fe-4S Clusters with a Free Coordination Site in Radical-SAM Enzymes JO: Front Chem http://www.kidney.de/pget.php?&tw=1&pmid=28361051 #FOAvip The canonical CysXXXCysXXCys motif is the hallmark of the Radical-SAM superfamily. This motif is responsible for the ligation of a [4Fe-4S] cluster containing a free coordination site available for SAM binding. The five enzymes MoaA, TYW1, MiaB, RimO and LipA contain in addition a second [4Fe-4S] cluster itself bound to three other cysteines and thus also displaying a potentially free coordination site. This review article summarizes recent important achievements obtained on these five enzymes with the main focus to delineate the role of this additional [4Fe-4S] cluster in catalysis. Twit Text FOAVip On the Role of Additional 4Fe-4S Clusters with a Free Coordination Site in Radical-SAM Enzymes ????Front Chem http://www.kidney.de/pget.php?&tw=1&pmid=28361051 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28361051 #FOAvip English Wikipedia <ref>{{Cite pmid|28361051}}</ref> On the Role of Additional 4Fe-4S Clusters with a Free Coordination Site in Radical-SAM Enzymes #MMPMID28361051 Mulliez E; Duarte V; Arragain S; Fontecave M; Atta M Front Chem 2017[]; 5 (ä): ä PMID28361051show ga The canonical CysXXXCysXXCys motif is the hallmark of the Radical-SAM superfamily. This motif is responsible for the ligation of a [4Fe-4S] cluster containing a free coordination site available for SAM binding. The five enzymes MoaA, TYW1, MiaB, RimO and LipA contain in addition a second [4Fe-4S] cluster itself bound to three other cysteines and thus also displaying a potentially free coordination site. This review article summarizes recent important achievements obtained on these five enzymes with the main focus to delineate the role of this additional [4Fe-4S] cluster in catalysis. äOn the Role of Additional 4Fe-4S Clusters with a Free Coordination S(epmc).pdf DeepDyve Pubget Overpricing