Zobrazeno 1 - 6
of 6
pro vyhledávání: '"35"'
Autor:
Dassama, Laura M. K.1,2, Silakov, Alexey1, Krest, Courtney M.1, Calixto, Julio C.1, Krebs, Carsten1,2 ckrebs@psu.edu, Martin Bollinger Jr., J.1,2 jmb21@psu.edu, Green, Michael T.1 mtg10@psu.edu
Publikováno v:
Journal of the American Chemical Society. 11/13/2013, Vol. 135 Issue 45, p16758-16761. 4p.
Autor:
Wörsdörfer, Bigna1, Conner, Denise A.1, Yokoyama, Kenichi2, Livada, Jovan1, Seyedsayamdost, Mohammad2, Wei Jiang1, Silakov, Alexey1,3 alexey.silakov@gmail.com, Stubbe, JoAnne2 stubbe@mit.edu, Bollinger Jr., J. Martin1,3 jmb21@psu.edu, Krebs, Carsten1,3 ckrebs@psu.edu
Publikováno v:
Journal of the American Chemical Society. 6/12/2013, Vol. 135 Issue 23, p8585-8593. 9p.
Publikováno v:
Journal of the American Chemical Society. 140:15744-15752
Class Ia ribonucleotide reductase (RNR) of Escherichia coli contains an unusually stable tyrosyl radical cofactor in the β2 subunit (Y122•) necessary for nucleotide reductase activity. Upon binding the cognate α2 subunit, loaded with nucleoside d
Publikováno v:
Journal of the American Chemical Society. 139:16657-16665
Ribonucleotide reductases (RNR) catalyze the reduction of nucleotides to deoxynucleotides through a mechanism involving an essential cysteine based thiyl radical. In the E. coli class 1a RNR the thiyl radical (C439•) is a transient species generate
Autor:
Alexey Silakov, Denise A. Conner, Wei Jiang, Mohammad R. Seyedsayamdost, Bigna Wörsdörfer, Kenichi Yokoyama, J. Martin Bollinger, JoAnne Stubbe, Carsten Krebs, Jovan Livada
Publikováno v:
Journal of the American Chemical Society. 135:8585-8593
The class Ia ribonucleotide reductase (RNR) from Escherichia coli (Ec) employs a free-radical mechanism, which involves bidirectional translocation of a radical equivalent or “hole” over a distance of ∼35 Å from the stable diferric/tyrosyl-rad
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