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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:
Peter E. Doan, Patricia C. Dos Santos, Hong-In Lee, Mikhail Laryukhin, Brian M. Hoffman, Lance C. Seefeldt, Dennis R. Dean, Robert Y. Igarashi
Publikováno v:
Journal of the American Chemical Society. 126:9563-9569
Nitrogenase is the metalloenzyme that catalyzes the nucleotide-dependent reduction of N(2), as well as reduction of a variety of other triply bonded substrates, including the alkyne, acetylene. Substitution of the alpha-70(Val) residue in the nitroge
Publikováno v:
Journal of the American Chemical Society. 132:2526-2527
We here report the first direct evidence addressing the possible involvement of Mo in substrate interactions during catalytic turnover. When the alpha-70(Ile) MoFe protein is freeze-trapped during H(+) reduction under Ar, the majority of the resting