Zobrazeno 1 - 10
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pro vyhledávání: '"35"'
Autor:
Kenneth M. Merz
Publikováno v:
Journal of the American Chemical Society. 113:3572-3575
Publikováno v:
Journal of the American Chemical Society. 125:11379-11384
Interdomain motions of Ca(2+)-ligated calmodulin were characterized by analyzing the nuclear magnetic resonance (15)N longitudinal relaxation rate R(1), transverse relaxation rate R(2), and steady-state {(1)H}-(15)N NOE of the backbone amide group at
Autor:
Dominique Florentin, Michel Azoulay, Jean-Claude Tabet, Georges Guillerm, François Frappier, Andrée Marquet
Publikováno v:
Journal of the American Chemical Society. 115:2139-2145
Previous results led to the conclusion that the last step of biotin biosynthesis, the sulfuur insertion into dethiobiotin should involve a thiol as intermediate. The three possible thiols have been synthesized and their biological activity was evalua
Publikováno v:
Journal of the American Chemical Society. 141:10821-10829
High fidelity human mitochondrial DNA polymerase (Pol γ) contains two active sites, a DNA polymerization site (pol) and a 3′−5′ exonuclease site (exo) for proofreading. Although separated by 35 Å, coordination between the pol and exo sites is
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
Autor:
Frank M. Raushel, Leisha S. Mullins
Publikováno v:
Journal of the American Chemical Society. 121:3803-3804
Ammonia can replace glutamine as the ultimate source for the nitrogen requirement in the reaction presented above.3 A chemical mechanism for the enzymatic transformation is presented below in Scheme 1. The first ATP phosphorylates bicarbonate to form
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
Publikováno v:
Journal of the American Chemical Society. 137:12343-12351
Four new chlorobromohydrins, mollenynes B-E, were isolated from the marine sponge Spirastrella mollis collected from Hogsty Reef, Bahamas. Their structures were elucidated by integrated analysis of NMR, MS, and computational methods. A high-resolutio
Autor:
John F. Quinn, Michael R. Whittaker, Phillip J. Hogg, Paul Wilson, Thomas P. Davis, Kristian Kempe, Sarah Mann, Athina Anastasaki, Angus P. R. Johnston, David M. Haddleton, Matthew R. Owen
Publikováno v:
Journal of the American Chemical Society. 137:4215-4222
The entropy-driven affinity of trivalent (in)organic arsenicals for closely spaced dithiols has been exploited to develop a novel route to peptide/protein-polymer conjugation. A trivalent arsenous acid (As(III)) derivative (1) obtained from p-arsanil
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