Localization of a Catalytic Intermediate Bound to the FeMo-cofactor of Nitrogenase

Nitrogenase catalyzes the biological reduction of N 2 to ammonia (nitrogen fixation) as well as the reduction of a number of alternative substrates, including acetylene (HCâ¡CH) to ethylene (H 2 C=CH 2 ). It is known that the metallocluster FeMo-cofactor located within the nitrogenase MoFe protein...

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Veröffentlicht in:	The Journal of biological chemistry 2004-08, Vol.279 (33), p.34770-34775
Hauptverfasser:	Igarashi, Robert Y, Dos Santos, Patricia C, Niehaus, Walter G, Dance, Ian G, Dean, Dennis R, Seefeldt, Lance C
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylene Alanine - chemistry Azotobacter Azotobacter vinelandii - enzymology Binding Sites Catalytic Domain Electron Spin Resonance Spectroscopy Histidine - chemistry Hydrogen-Ion Concentration Imidazoles - chemistry Iron Kinetics Magnetics Models, Chemical Models, Molecular Molybdoferredoxin - chemistry Nitrogenase - chemistry Protein Binding Valine - chemistry
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