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pro vyhledávání: '"35"'
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:
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
Autor:
Stoyan K. Smoukov, Brian M. Hoffman, Stephen J. Lippard, Daniel A. Kopp, Roman Davydov, Ann M. Valentine
Publikováno v:
Journal of the American Chemical Society. 124:2657-2663
The binding of ethanol and 1,1,1-trifluoroethanol (TFE) to both the H(mv) and H(ox) forms of soluble methane monooxygenase (sMMO) in solution has been studied by Q-band (35 GHz) CW and pulsed ENDOR spectroscopy of (1)H, (2)H and (19)F nuclei of exoge