Zobrazeno 61 - 68
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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. 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
Autor:
Robert G. Griffin, Sylwia Kacprzak, Brian Hoffman, Erin Artin, JoAnne Stubbe, Hendrik Zipse, Debora Marcela Martino, Nicholas Lees, Martin Kaupp, Gregory J. S. Lohman, Marina Bennati, Stanislaw F. Wnuk
Publikováno v:
Journal of the American Chemical Society
The Escherichia coli ribonucleotide reductase (RNR) catalyzes the conversion of nucleoside diphosphates to deoxynucleotides and requires a diferric-tyrosyl radical cofactor for catalysis. RNR is composed of a 1:1 complex of two homodimeric subunits:
Publikováno v:
Journal of the American Chemical Society. 128(24)
Simulations of hydride and deuteride transfer catalyzed by dihydrofolate reductase from the hyperthermophile Thermotoga maritima (TmDHFR) are presented. TmDHFR was modeled with its active homodimeric quaternary structure, where each monomer has three
Autor:
JoAnne Stubbe, Peter P. Borbat, Marina Bennati, Veronica Mugnaini, Jack H. Freed, John H. Robblee
Publikováno v:
Journal of the American Chemical Society. 127(43)
The class I E. coli ribonucleotide reductase, composed of homodimers of R1 and R2, catalyzes the conversion of nucleoside diphosphates to deoxynucleoside diphosphates. The reduction process involves the tyrosyl radical on R2 that generates a transien
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
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. 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