Substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis
BM Barney, RY Igarashi, PC Dos Santos… - Journal of Biological …, 2004 - ASBMB
Nitrogenase catalyzes biological dinitrogen fixation, the reduction of N 2 to 2NH 3. Recently,
the binding site for a non-physiological alkyne substrate (propargyl alcohol, HC≡ C-CH 2
OH) was localized to a specific Fe-S face of the FeMo-cofactor approached by the MoFe
protein amino acid α-70 Val. Here we provide evidence to indicate that the smaller alkyne
substrate acetylene (HC≡ CH), the physiological substrate dinitrogen, and its semi-reduced
form hydrazine (H 2 N-NH 2) interact with the same Fe-S face of the FeMo-cofactor …
the binding site for a non-physiological alkyne substrate (propargyl alcohol, HC≡ C-CH 2
OH) was localized to a specific Fe-S face of the FeMo-cofactor approached by the MoFe
protein amino acid α-70 Val. Here we provide evidence to indicate that the smaller alkyne
substrate acetylene (HC≡ CH), the physiological substrate dinitrogen, and its semi-reduced
form hydrazine (H 2 N-NH 2) interact with the same Fe-S face of the FeMo-cofactor …
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