Zobrazeno 1 - 10
of 21
pro vyhledávání: '"35"'
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
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
Autor:
Matthew O. Ross, Igor D. Petrik, Pierre Moënne-Loccoz, Yelu Shi, Yi Lu, Qianhong Zhu, Ambika Bhagi-Damodaran, Julian Reed, Yong Zhang, Saumen Chakraborty, Evan N. Mirts
Publikováno v:
Journal of the American Chemical Society. 139(35)
The presence of nonheme metal, such as copper and iron, in the heme-copper oxidase (HCO) superfamily is critical to the enzymatic activity of reducing O2 to H2O, but the exact mechanism the nonheme metal ion uses to confer and fine-tune the activity
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
Publikováno v:
Journal of the American Chemical Society. 133:19807-19815
S-adenosylhomocysteine hydrolase (SAHH), a cellular enzyme that plays a key role in methylation reactions including those required for maturation of viral mRNA, is an important drug target in the discovery of antiviral agents. While targeting the act
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
Ribonucleotide reductases (RNRs) catalyze the conversion of nucleotides to deoxynucleotides in all organisms. Active E. coli class Ia RNR is an α2β2 complex that undergoes reversible, long-range proton-coupled electron transfer (PCET) over a pathwa
Publikováno v:
Journal of the American Chemical Society, 125(35), 10570-10579. AMER CHEMICAL SOC
The binding of a series of p-alkylbenzamidinium chloride inhibitors to the serine proteinase trypsin over a range of temperatures has been studied using isothermal titration (micro)calorimetry and molecular dynamics simulation techniques. The inhibit
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
Publikováno v:
Journal of the American Chemical Society. 119:3853-3860
Recent kinetic measurements of the oxidation of linoleic acid by soybean lipoxygenase show that the thermal rate constants, kH ) 280 ((12) s -1 and kD ) 5.0 ((0.1) s -1 , are weakly temperature dependent within the temperature interval 30-50 °C. The