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Iron-molybdenum cofactor from nitrogenase. Modified extraction methods as probes for composition.

S S Yang, W H Pan, G D Friesen

    The Journal of Biological Chemistry
    |July 25, 1982
    PubMed
    Summary

    New methods for isolating the iron-molybdenum cofactor (FeMoco) from nitrogenase show pH is key. These FeMoco isolation techniques yield stable cofactors with consistent activity and composition, revealing insights into its structure.

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    Area of Science:

    • Biochemistry
    • Bioinorganic Chemistry
    • Enzymology

    Background:

    • The molybdenum-iron (MoFe) protein of nitrogenase contains the iron-molybdenum cofactor (FeMoco), crucial for biological nitrogen fixation.
    • Understanding FeMoco's structure and stability is vital for improving nitrogenase activity and nitrogen fixation efficiency.

    Purpose of the Study:

    • To develop and evaluate modified preparative procedures for isolating FeMoco from Azotobacter vinelandii nitrogenase.
    • To determine the essential components for FeMoco isolation and stability and investigate the role of pH.

    Main Methods:

    • Developed five modified procedures for isolating FeMoco.
    • Analyzed FeMoco yield, metal composition, charge, EPR spectra, and specific activity after reconstitution.
    • Investigated the effect of various reagents (Tris, Cl-, citrate, HPO4(2-), N,N-dimethylformamide, N-methylformamide) and pH on FeMoco isolation and stability.

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    Main Results:

    • No single component of the original isolation protocol is essential for FeMoco isolation or stability, though they can act as ligands.
    • Effective isolation is highly dependent on the pH of the extracting solvent.
    • New procedures yielded FeMoco with properties (metal analysis, EPR, activity) comparable to the original method.
    • Purified FeMoco has a Mo:Fe:S ratio of approximately 1:7:4 with N-methylformamide as a ligand, lacking endogenous organic components.
    • Quantification of iron using o-phenanthroline revealed a consistent relationship between FeMoco-associated iron and specific activity.

    Conclusions:

    • FeMoco isolation is robust and adaptable, with pH being a critical parameter.
    • The coordination sphere of FeMoco appears labile and influenced by exogenous ligands rather than endogenous organic components.
    • Further investigation into the coordination sphere's nature is warranted.