The Chemical Evolution of a Nitrogenase Model, XXIII. The Nature of the Active Site and the Role of Homocitric Acid in MoFe-Nitrogenase
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چکیده
The iron-molybdenum cofactor (FeMo-co) of bacterial nitrogenase is a heterometallic cluster of composition MoFe7S9 that is attached to the apoprotein by a coordinative Mo-N bond to the imidazole group of hisa442, and by a Fe-S bond to cysa.215. The molybdenum atom of FeMo-co in the enzyme in addition is coordinated to one molecule of homocitrate (he), which is required for maximal N2 reducing activity. The molybdenum atom in the enzyme-bound FeMo-co thus is hexacoordinated and cannot react with substrates unless free coordination sites are made available. It is proposed that the reactions of the substrates of nitrogenase occur at a molybdenum active site consisting of a mononuclear molybdenum homocitrate complex attached to hisaAA2 of the apoprotein that in the functional enzyme is generated from FeMo-co by a reversible, redox-linked dissociation of the Fe7S9-c;y5' cluster. Studies with catalytic model systems consisting of complexes of molybdenum with imidazole and hydroxocarboxylate ligands support this proposal and provide a rationale for the specific activating effect of homocitrate in nitrogenase.
منابع مشابه
Nitrogenase from nifV mutants of Klebsiella pneumoniae contains an altered form of the iron-molybdenum cofactor.
When the iron-molybdenum cofactor (FeMoco) was extracted from the MoFe protein of nitrogenase from a nifV mutant of Klebsiella pneumoniae and combined with the FeMoco-deficient MoFe protein from a nifB mutant, the resultant MoFe protein exhibited the NifV phenotype, i.e. in combination with wild-type Fe protein it exhibited poor N2-fixation activity and its H2-evolution activity was inhibited b...
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