Zobrazeno 1 - 5
of 5
pro vyhledávání: '"35"'
Autor:
R. Adam Kinney, Bo Zhang, Rebecca L. McNaughton, Russ Hille, Muralidharan Shanmugam, Brian M. Hoffman
Publikováno v:
Journal of the American Chemical Society. 132:14015-14017
The formaldehyde-inhibited Mo(V) state of xanthine oxidase (I) has been studied for four decades, yet it has not proven possible to distinguish unequivocally among the several structures proposed for this form. The uniquely large isotropic hyperfine
Autor:
Petra Hänzelmann, Sowmya Subramanian, Michael K. Johnson, Brian M. Hoffman, Heather L. Hernandez, Hermann Schindelin, Nicholas S. Lees
Publikováno v:
Journal of the American Chemical Society. 131:9184-9185
The S-adenosylmethionine-dependent enzyme MoaA, in concert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of guanosine 5'-triphosphate (5'-GTP) into precursor Z. A published X-ray crystal structure of MoaA wit
Autor:
Brian M. Hoffman, Joshua Telser, Brett M. Barney, Peter E. Doan, Lance C. Seefeldt, Robert Y. Igarashi, Dennis R. Dean
Publikováno v:
Journal of the American Chemical Society. 133:17329-17340
N(2) binds to the active-site metal cluster in the nitrogenase MoFe protein, the FeMo-cofactor ([7Fe-9S-Mo-homocitrate-X]; FeMo-co) only after the MoFe protein has accumulated three or four electrons/protons (E(3) or E(4) states), with the E(4) state
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:
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