Zobrazeno 1 - 7
of 7
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. 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. 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. 129(51)
It was recently suggested that partially reduced monoamine oxidase (MAO) A contains an equilibrium mixture of an anionic flavin radical and a tyrosyl radical (Rigby, S. E.; et al. J. Biol. Chem. 2005, 280, 4627-4632). These observations formed the ba
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