Zobrazeno 1 - 10
of 11
pro vyhledávání: '"35"'
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
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
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. 125:14728-14732
The description of reaction regulation in enzymes responsible for activating and catalyzing small molecules (O(2), NO) requires identification of ligand movement into the binding site and out of the enzyme through specific channels and docking sites.
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. 126(39)
A variety of spectroscopic and computational techniques have been used to examine the thermochromic transition previously reported for the oxidized state of Mn-dependent superoxide dismutase from E. coli in the presence of substrate analog azide (N(3
Autor:
Richard N. Armstrong, Christopher L. Rife, Stoyan K. Smoukov, Joshua Telser, Brian M. Hoffman, Bryan A Bernat
Publikováno v:
Journal of the American Chemical Society. 124(10)
FosA is a manganese metalloglutathione transferase that confers resistance to the broad-spectrum antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid. The reaction catalyzed by FosA involves the attack by glutathione on fosfomycin to yield the p
Autor:
Allen M. Orville, Jeffrey M. Zaleski, Edward I. Solomon, Mindy I. Davis, Frank Neese, John D. Lipscomb
Publikováno v:
Journal of the American Chemical Society. 124(4)
The geometric and electronic structure of the high-spin ferric active site of protocatechuate 3,4-dioxygenase (3,4-PCD) has been examined by absorption (Abs), circular dichroism (CD), magnetic CD (MCD), and variable-temperature-variable-field (VTVH)
Autor:
Stephen G. Withers, David K. Y. Poon, Mario Schubert, Lawrence P. McIntosh, Mark Okon, Jason Au
Publikováno v:
Journal of the American Chemical Society. 128:15388-15389
We have investigated the lysine side chain amines in the 34 kDa catalytic domain from Cellulomonas fimi beta-(1,4)-glycosidase Cex (or CfXyn10A) using 1H-detected 15N heteronuclear correlation NMR spectroscopy. Signals from the 1Hzeta ( approximately