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pro vyhledávání: '"35"'
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
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
Autor:
Koichiro Ishimori, Isao Morishima, Takehiko Tosha, Shiro Yoshioka, Hiroshi Hori, Satoshi Takahashi
Publikováno v:
Journal of the American Chemical Society. 124:14571-14579
Structural and functional roles of the hydrogen bonding network that surrounds the heme-thiolate coordination of P450(cam) from Pseudomonas putida were investigated. A hydrogen bond between the side chain amide of Gln360 and the carbonyl oxygen of th
Publikováno v:
Journal of the American Chemical Society. 127(23)
FosA is a manganese metalloglutathione transferase that confers resistance to the broad-spectrum antibiotic fosfomycin, which contains a phosphonate group. The active site of this enzyme consists of a high-spin Mn(2+) ion coordinated by endogenous li
Autor:
Stephen G. Withers, David K. Y. Poon, Mario Schubert, Lawrence P. McIntosh, Mark Okon, Jason Au
Publikováno v:
Journal of the American Chemical Society. 128:15388-15389
We have investigated the lysine side chain amines in the 34 kDa catalytic domain from Cellulomonas fimi beta-(1,4)-glycosidase Cex (or CfXyn10A) using 1H-detected 15N heteronuclear correlation NMR spectroscopy. Signals from the 1Hzeta ( approximately