Zobrazeno 1 - 4
of 4
pro vyhledávání: '"35"'
Autor:
Yao H; Department of Chemistry, University of Kansas, Multidisciplinary Research Building, 2030 Becker Drive, Lawrence, Kansas 66047, USA., Wang Y, Lovell S, Kumar R, Ruvinsky AM, Battaile KP, Vakser IA, Rivera M
Publikováno v:
Journal of the American Chemical Society [J Am Chem Soc] 2012 Aug 15; Vol. 134 (32), pp. 13470-81. Date of Electronic Publication: 2012 Aug 01.
Publikováno v:
Journal of the American Chemical Society. 134:2520-2523
The reaction of a class I ribonucleotide reductase (RNR) begins when a cofactor in the β subunit oxidizes a cysteine residue ~35 Å away in the α subunit, generating a thiyl radical. In the class Ic enzyme from Chlamydia trachomatis (Ct), the cyste
Autor:
Julio C. Calixto, Michael Green, Laura M. K. Dassama, J. Martin Bollinger, Alexey Silakov, Courtney M. Krest, Carsten Krebs
Publikováno v:
Journal of the American Chemical Society. 135(45)
A class Ia ribonucleotide reductase (RNR) employs a μ-oxo-Fe2(III/III)/tyrosyl radical cofactor in its β subunit to oxidize a cysteine residue ~35 A away in its α subunit; the resultant cysteine radical initiates substrate reduction. During self-a
Autor:
Ana Pamplona, David L. Tierney, José J. G. Moura, Carlos D. Brondino, Marta S. P. Carepo, Joshua Telser, Brian M. Hoffman, Tran Chin Yang, Isabel Moura
Publikováno v:
Journal of the American Chemical Society. 124(2)
Crystallographic studies of the hydrogenases (Hases) from Desulfovibrio gigas (Dg) and Desulfovibrio vulgaris Miyazaki (DvM) have revealed heterodinuclear nickel-iron active centers in both enzymes. The structures, which represent the as-isolated (un