Zobrazeno 31 - 40
of 125
pro vyhledávání: '"35"'
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:
Michal Avital-Shmilovici, Kalyaneswar Mandal, Nelson B. Phillips, Michael A. Weiss, Zachary P. Gates, Stephen B. H. Kent
Publikováno v:
Journal of the American Chemical Society. 135:3173-3185
Efficient total synthesis of insulin is important to enable the application of medicinal chemistry to the optimization of the properties of this important protein molecule. Recently we described "ester insulin"--a novel form of insulin in which the f
Publikováno v:
Journal of the American Chemical Society. 138(22)
Circular bacteriocins, ranging from 35 to 70 amino acids, are the largest cyclic peptides produced by lactic acid bacteria to suppress growth of other bacteria. Their end-to-end cyclized backbone that enhances molecular stability is an advantage to s
Publikováno v:
Journal of the American Chemical Society. 134:11952-11955
Oligosaccharide synthesis is hindered by the need for multiple steps as well as numerous selective protections and deprotections. Herein we report a highly efficient de novo route to various oligosaccharide motifs, of use for biological and medicinal
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. 133:18420-18432
Escherichia coli ribonucleotide reductase is an α2β2 complex that catalyzes the conversion of nucleotides to deoxynucleotides using a diferric tyrosyl radical (Y(122)(•)) cofactor in β2 to initiate catalysis in α2. Each turnover requires revers
Publikováno v:
Journal of the American Chemical Society. 132:587-595
Synthetic biology and systems chemistry demonstrate a growing interest in modified nucleotides to achieve an enzymatically stable artificial nucleic acid. A potential candidate system is xylose-DNA, in which the 2'-deoxy-beta-D-ribo-furanose is subst
Autor:
Mohammad R. Seyedsayamdost, Tomislav Argirević, JoAnne Stubbe, Ellen Catherine Minnihan, Marina Bennati
Publikováno v:
Journal of the American Chemical Society
E. coli ribonucleotide reductase (RNR) catalyzes the conversion of nucleotides to deoxynucleotides, a process that requires long-range radical transfer over 35 A from a tyrosyl radical (Y(122)*) within the beta2 subunit to a cysteine residue (C(439))
Publikováno v:
Journal of the American Chemical Society. 131:10406-10420
Reaction of UCl(4)(THF)(4) with 1,3-[2,5-(i-Pr)(2)PhNC( horizontal lineCH(2))](2)C(6)H(4)Li(2) produced a complex formulated as [{1,3-[2,5-(i-Pr)(2)PhNC( horizontal lineCH(2))](2)C(6)H(4)}UCl(3)][Li(THF)(4)] (1) that exhibits a nonagostic interaction
Autor:
Martin J. Stillman, Thanh T. Ngu
Publikováno v:
Journal of the American Chemical Society. 128:12473-12483
The number of reported cases of chronic arsenic poisoning is on the rise throughout the world, making the study of the long-term effects of arsenic critical. As(3+) binds readily to biological thiols, including mammalian metallothionein (MT), which i