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Recent crystallographic analysis of the metal centers in the nitrogenasemolybdenum-iron protein with 0.22 and 0.27 nm resolution revealed the structural model ofFeMo-cofactor as a cage-like cluster, in which molybdenum is chelated by hydroxy- andcarboxylate ligands of homocitrate. It is deduced that the homocitrate may be importantfor the substrate reduction mechanism. Considering that the central molybdenum of nitrogenase
Recent crystallographic analysis of the metal centers in the nitrogenase molybdenum-iron protein with 0.22 and 0.27 nm resolution revealed the structural model of FeMo-cofactor as a cage-like cluster, in which molybdenum is chelated by hydroxy- and carboxylate ligands of homocitrate. It is deduced that the homocitrate may be important for the substrate reduction mechanism. Considering that the central molybdenum of nitrogenase