Itoh Group Literature Review

Ilija  Č ori ć , Brandon Q. Mercado , Eckhard Bill , David J. Vinyard &  Patrick L. Holland Nature   526 ,   96–99   (01 October 2015)   doi:10.1038/nature15246 Received   27 May 2015  Accepted   24 July 2015  Published online   23 September 2015 http://www.nature.com/nature/journal/v526/n7571/full/nature15246.html Abstract Nitrogenases are the enzymes by which certain microorganisms convert atmospheric dinitrogen (N 2 ) to ammonia, thereby providing essential nitrogen atoms for higher organisms. The most common nitrogenases reduce atmospheric N 2  at the FeMo cofactor, a sulfur-rich iron–molybdenum cluster (FeMoco) 1 ,  2 ,  3 ,  4 ,  5 . The central iron sites that are coordinated to sulfur and carbon atoms in FeMoco have been proposed to be the substrate binding sites, on the basis of kinetic and spectroscopic studies 5 ,  6 ,  7 . In the resting state, the central iro...

by John A. McIntosh, Thomas Heel, Andrew R. Buller, Linda Chio and Frances H. Arnold  /  16h  //  keep unread  //  hide  //  preview http://pubs.acs.org/doi/10.1021/jacs.5b07107 http://pubs.acs.org/doi/pdf/10.1021/jacs.5b07107 Journal of the American Chemical Society DOI: 10.1021/jacs.5b07107 Visit Website

Nature Chemistry by Courtney M. Krest  /  20h  //  keep unread  //  hide  //  preview http://www.nature.com/nchem/journal/vaop/ncurrent/pdf/nchem.2306.pdf Nature Chemistry. doi:10.1038/nchem.2306 Authors: Courtney M. Krest, Alexey Silakov, Jonathan Rittle, Timothy H. Yosca, Elizabeth L. Onderko, Julio C. Calixto & Michael T. Green Cytochrome P450 (P450) and chloroperoxidase (CPO) are both thiolate-ligated haem proteins that form a ferryl radical species called compound I. P450-I is, however, significantly more reactive than CPO-I. Variable-temperature Mössbauer and X-ray absorption measurements have now shown that increased electron donation from the axial thiolate ligand in P450-I may explain its greater propensity for C–H bond activation. Visit Website

RSC - Dalton Trans. latest articles  by Erica C. M. Ording-Wenker  /   30d   //   keep unread   //   hide   //   preview Dalton Trans. , 2015, Advance Article DOI : 10.1039/C5DT01041A, Paper Erica C. M. Ording-Wenker, Maxime A. Siegler, Martin Lutz, Elisabeth Bouwman High activity for the catalytic oxidation of 3,5-di- tert -butylcatechol was achieved with complexes of ligands that stabilize the biomimetic Cu II  [small mu]-thiolate complex, hinting at a similarity with the required Cu-oxo intermediates. To cite this article before page numbers are assigned, use the DOI form of citation above. The content of this RSS Feed (c) The Royal Society of Chemistry Visit Website