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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
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
Publikováno v:
Journal of the American Chemical Society. 122:182-183
Methyl-coenzyme M reductase (MCR) catalyzes the chemical step of methane formation by methanogenic organisms. The reaction involves the two-electron reduction of CH{sub 3}S-CoM by N-7-mercaptoheptanoylthreoinine phosphate (CoB-SH). The authors have e