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pro vyhledávání: '"35"'
Publikováno v:
Journal of the American Chemical Society. 105:7337-7345
Studies have been conducted on the ground-state and excited-state solvolyses of the isomeric 7,8-dichloro derivatives of benzonaphthobicyclo(2.2.2)octadiene and benzoveratrobicyclo(2.2.2)octadiene. The silver ion assisted ground-state reactions proce
Publikováno v:
Journal of the American Chemical Society. 106:2483-2483
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. 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•
Autor:
Mohammad R. Seyedsayamdost, Bridgette A. Barry, I. R. Vassiliev, Adam R. Offenbacher, JoAnne Stubbe
Publikováno v:
Journal of the American Chemical Society. 131:7496-7497
Ribonucleotide reductase (RNR) catalyzes the reduction of ribonucleotides to deoxyribonucleotides.1–3 Class I RNRs are composed of a 1:1 complex of two homodimeric proteins, α2 and β2. α2 contains the binding site for substrates and allosteric e