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pro vyhledávání: '"35"'
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
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
Autor:
Stoyan K. Smoukov, Brian M. Hoffman, Stephen J. Lippard, Daniel A. Kopp, Roman Davydov, Ann M. Valentine
Publikováno v:
Journal of the American Chemical Society. 124:2657-2663
The binding of ethanol and 1,1,1-trifluoroethanol (TFE) to both the H(mv) and H(ox) forms of soluble methane monooxygenase (sMMO) in solution has been studied by Q-band (35 GHz) CW and pulsed ENDOR spectroscopy of (1)H, (2)H and (19)F nuclei of exoge
Autor:
E. C. Abresch, and Melvin Y. Okamura, George Feher, Rafael Calvo, Mark L. Paddock, Wolfgang Lubitz, Wulf Hofbauer, Robert Bittl, R.A. Isaacson
Publikováno v:
Journal of the American Chemical Society. 122:7327-7341
The photocycle of bacterial photosynthetic reaction centers (RCs) involves electron transfer between two quinone molecules, QA and QB. The semiquinone biradical QA-•QB-• forms an intermediate state in this process. We trapped the biradical at low
Publikováno v:
Journal of the American Chemical Society. 119:3853-3860
Recent kinetic measurements of the oxidation of linoleic acid by soybean lipoxygenase show that the thermal rate constants, kH ) 280 ((12) s -1 and kD ) 5.0 ((0.1) s -1 , are weakly temperature dependent within the temperature interval 30-50 °C. The
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