Zobrazeno 1 - 10
of 10
pro vyhledávání: '"35"'
Autor:
Cui C; Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, United States., Song DY; Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, United States., Drennan CL; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.; Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.; Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States., Stubbe J; Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, United States.; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.; Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States., Nocera DG; Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, United States.
Publikováno v:
Journal of the American Chemical Society [J Am Chem Soc] 2023 Mar 08; Vol. 145 (9), pp. 5145-5154. Date of Electronic Publication: 2023 Feb 22.
Autor:
Argirević T; Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany., Riplinger C, Stubbe J, Neese F, Bennati M
Publikováno v:
Journal of the American Chemical Society [J Am Chem Soc] 2012 Oct 24; Vol. 134 (42), pp. 17661-70. Date of Electronic Publication: 2012 Oct 16.
Autor:
Wörsdörfer B; Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802, USA., Conner DA, Yokoyama K, Livada J, Seyedsayamdost M, Jiang W, Silakov A, Stubbe J, Bollinger JM Jr, Krebs C
Publikováno v:
Journal of the American Chemical Society [J Am Chem Soc] 2013 Jun 12; Vol. 135 (23), pp. 8585-93. Date of Electronic Publication: 2013 May 31.
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
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. 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. 131(9)
We previously used a combination of CW and pulsed-ENDOR protocols to identify the types of protonated oxygen (OHx) species and their disposition within the FeIII/FeIV cluster of Intermediate X, the direct precursor of the essential diferric-tyrosyl r
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•