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pro vyhledávání: '"35"'
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
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
Autor:
Ana Pamplona, David L. Tierney, José J. G. Moura, Carlos D. Brondino, Marta S. P. Carepo, Joshua Telser, Brian M. Hoffman, Tran Chin Yang, Isabel Moura
Publikováno v:
Journal of the American Chemical Society. 124(2)
Crystallographic studies of the hydrogenases (Hases) from Desulfovibrio gigas (Dg) and Desulfovibrio vulgaris Miyazaki (DvM) have revealed heterodinuclear nickel-iron active centers in both enzymes. The structures, which represent the as-isolated (un