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Publikováno v:
Journal of the American Chemical Society. 125:11379-11384
Interdomain motions of Ca(2+)-ligated calmodulin were characterized by analyzing the nuclear magnetic resonance (15)N longitudinal relaxation rate R(1), transverse relaxation rate R(2), and steady-state {(1)H}-(15)N NOE of the backbone amide group at
Publikováno v:
Journal of the American Chemical Society. 137:12343-12351
Four new chlorobromohydrins, mollenynes B-E, were isolated from the marine sponge Spirastrella mollis collected from Hogsty Reef, Bahamas. Their structures were elucidated by integrated analysis of NMR, MS, and computational methods. A high-resolutio
Publikováno v:
Journal of the American Chemical Society. 119:10121-10126
The resting state of nitrogenase shows an S = 3/2 electron paramagnetic resonance (EPR) signal resulting from the FeMo-cofactor (MoFe7S9:homocitrate) of the MoFe protein. When the enzyme undergoes turnover under a CO atmosphere, this signal disappear
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