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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
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
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
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. 132(43)
Escherichia coli ribonucleotide reductase is an α2β2 complex that catalyzes the conversion of nucleotides to deoxynucleotides and requires a diferric-tyrosyl radical (Y(•)) cofactor to initiate catalysis. The initiation process requires long-rang
Publikováno v:
Journal of the American Chemical Society. 132(24)
E. coli ribonucleotide reductase catalyzes the reduction of nucleoside 5'-diphosphates into 2'-deoxynucleotides and is composed of two subunits: alpha2 and beta2. During turnover, a stable tyrosyl radical (Y*) at Y(122)-beta2 reversibly oxidizes C(43
Publikováno v:
Journal of the American Chemical Society. 125(35)
Escherichia coli class I ribonucleotide reductase catalyzes the conversion of ribonucleotides to deoxyribonucleotides and consists of two subunits: R1 and R2. R1 possesses the active site, while R2 harbors the essential diferric-tyrosyl radical (Y•
Publikováno v:
Journal of the American Chemical Society. 114:2277-2279
The recent isolation of fullerenes such as C{sub 60} and C{sub 70} has led to several studies of the reactivity and physical properties of their excited states. The authors recently reported that triplet C{sub 60} ({sup 3}C{sub 60}) is formed with a
Publikováno v:
Journal of the American Chemical Society. 128:2522-2523
E. coli ribonucleotide reductase (RNR), composed of the homodimeric subunits alpha2 and beta2, catalyzes the conversion of nucleotides to deoxynucleotides via complex radical chemistry. The radical initiation process involves a putative proton-couple