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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:
Jordi Benet-Buchholz, Teodor Parella, T. Daniel P. Stack, Xavi Ribas, Albert Poater, Alicia Casitas, Carlos Calle, Antoni Llobet, Raül Xifra, A. Schweiger, Miquel Solà, George Mitrikas, Laura Gómez
Publikováno v:
© Journal of the American Chemical Society, 2010, vol. 132, núm. 35, p. 12299-12306
Articles publicats (D-Q)
DUGiDocs – Universitat de Girona
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Articles publicats (D-Q)
DUGiDocs – Universitat de Girona
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The present study provides mechanistic details of a mild aromatic C-H activation effected by a copper(II) center ligated in a triazamacrocylic ligand, affording equimolar amounts of a CuIII-aryl species and CuIspecies as reaction products. At low tem
Publikováno v:
Journal of the American Chemical Society
Ribonucleotide reductases (RNRs) catalyze the conversion of ribonucleotides to deoxyribonucleotides in all organisms. In all Class Ia RNRs, initiation of nucleotide diphosphate (NDP) reduction requires a reversible oxidation over 35 Å by a tyrosyl r
Publikováno v:
Journal of the American Chemical Society. 125(35)
Escherichia coli class I ribonucleotide reductase catalyzes the conversion of ribonucleotides to deoxyribonucleotides and consists of two subunits: R1 and R2. R1 possesses the active site, while R2 harbors the essential diferric-tyrosyl radical (Y•