Zobrazeno 1 - 3
of 3
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.
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