Zobrazeno 101 - 110
of 125
pro vyhledávání: '"35"'
Autor:
William E. Broderick, Brian M. Hoffman, Joan B. Broderick, Charles J. Walsby, Jennifer Cheek, Danilo Ortillo, Wei Hong
Publikováno v:
Journal of the American Chemical Society. 124(12)
Pyruvate formate-lyase activating enzyme (PFL-AE) is a representative member of an emerging family of enzymes that utilize iron-sulfur clusters and S-adenosylmethionine (AdoMet) to initiate radical catalysis. Although these enzymes have diverse funct
Publikováno v:
Journal of the American Chemical Society. 124(11)
Despite the current availability of several crystal structures of purple acid phosphatases, to date there is no direct evidence for solvent-derived ligands occupying terminal positions in the active enzyme. This is of central importance, because cata
Autor:
Richard N. Armstrong, Christopher L. Rife, Stoyan K. Smoukov, Joshua Telser, Brian M. Hoffman, Bryan A Bernat
Publikováno v:
Journal of the American Chemical Society. 124(10)
FosA is a manganese metalloglutathione transferase that confers resistance to the broad-spectrum antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid. The reaction catalyzed by FosA involves the attack by glutathione on fosfomycin to yield the p
Autor:
Allen M. Orville, Jeffrey M. Zaleski, Edward I. Solomon, Mindy I. Davis, Frank Neese, John D. Lipscomb
Publikováno v:
Journal of the American Chemical Society. 124(4)
The geometric and electronic structure of the high-spin ferric active site of protocatechuate 3,4-dioxygenase (3,4-PCD) has been examined by absorption (Abs), circular dichroism (CD), magnetic CD (MCD), and variable-temperature-variable-field (VTVH)
Publikováno v:
Journal of the American Chemical Society. 123(11)
Streptomyces coelicolor CH999/pJRJ2 harbors a plasmid encoding DEBS(KS1 degrees ), a mutant form of 6-deoxyerythronolide B synthase that is blocked in the formation of 6-deoxyerythronolide B (1, 6-dEB) due to a mutation in the active site of the keto
Publikováno v:
Journal of the American Chemical Society. 123(3)
We have characterized, for the first time, motional modes of a protein dissolved in supercooled water: the flipping kinetics of phenylalanyl and tyrosinyl rings of the 6 kDa protein BPTI have been investigated by NMR at temperatures between -3 and -1
Publikováno v:
Journal of the American Chemical Society. 123(25)
Concise syntheses of the Ergot alkaloids rugulovasine A (3a), rugulovasine B (3b), and setoclavine (2) have been completed by strategies that feature inter- and intramolecular vinylogous Mannich reactions as the key steps. Thus, the first synthesis o
Autor:
Mohammad R. Seyedsayamdost, Bridgette A. Barry, I. R. Vassiliev, Adam R. Offenbacher, JoAnne Stubbe
Publikováno v:
Journal of the American Chemical Society. 131:7496-7497
Ribonucleotide reductase (RNR) catalyzes the reduction of ribonucleotides to deoxyribonucleotides.1–3 Class I RNRs are composed of a 1:1 complex of two homodimeric proteins, α2 and β2. α2 contains the binding site for substrates and allosteric e
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
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