Itoh Group Literature Review

http://www.nature.com/nchembio/journal/v12/n1/full/nchembio.1976.html Rhiannon M Evans , Emily J Brooke , Sara A M Wehlin , Elena Nomerotskaia , Frank Sargent , Stephen B Carr , Simon E V Phillips &  Fraser A Armstrong Affiliations Contributions Corresponding authors Nature Chemical Biology   Nature Chemical Biology   12 ,   46–50   (2016)   doi:10.1038/nchembio.1976 Received 25 June 2015  Accepted 26 October 2015  Published online 30 November 2015 Article tools Abstract The active site of [NiFe] hydrogenases contains a strictly conserved arginine that suspends a guanidine nitrogen atom <4.5 Å above the nickel and iron atoms. The guanidine headgroup interacts with the side chains of two conserved aspartic acid residues to complete an outer-shell canopy that has thus far proved intractable to investigation by site-directed mutagenesis. Using hydrogenase-1 from  Escherichia coli...

NATURE CHEMICAL BIOLOGY  |  ARTICLE Print Share/bookmark Po-ssu Huang 1,2,6 *, Kaspar Feldmeier 3,6 , Fabio Parmeggiani 1,2 , D Alejandro Fernandez Velasco 4 , Birte Höcker 3 * & David Baker 1,2,5 *  1 department of biochemistry, university of Washington, Seattle, Washington, uSA. 2 institute for protein design, university of Washington, Seattle, Washington, uSA. 3 Max planck institute for developmental biology, tübingen, Germany. 4 Facultad de Medicina, universidad nacional Autónoma de México (unAM), ciudad universitaria, México dF, Mexico. 5 Howard Hughes Medical institute, university of Washington, Seattle, Washington, uSA. DOI:10.1038/nchembio.1966 Despite efforts for over 25 years, de novo protein design has not succeeded in achieving the TIM-barrel fold. Here we describe the computational design of four-fold symmetrical ( b / a ) 8 barrels guided by geometrical and ch...

tobias Weinert 1,8 , simona G Huwiler 2,8 , johannes W Kung 2 , sina Weidenweber 1 , petra Hellwig 3 , Hans-joachim stärk 4 , till Biskup 5 , stefan Weber 5 , julien j H Cotelesage 6,7 , Graham n George 6 , ulrich ermler 1 * & Matthias Boll 2 *  Nature Chemical Biology (2015) 　doi:10.1038/nchembio.1849 Received 13 January 2015   Accepted 15 May 2015 http://www.nature.com/nchembio/journal/vaop/ncurrent/full/nchembio.1849.html   In chemical synthesis, the widely used Birch reduction of aromatic compounds to cyclic dienes requires alkali metals in ammo- nia as extremely low-potential electron donors. An analogous reaction is catalyzed by benzoyl–coenzyme A reductases (BCRs) that have a key role in the globally important bacterial degradation of aromatic compounds at anoxic sites. Because of the lack of structural information, the catalytic mechanism of enzymatic benzene ring r...