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Related Experiment Videos

The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures

M K Chan1, J Kim, D C Rees

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.

Science (New York, N.Y.)
|May 7, 1993
PubMed
Summary

Crystallographic verification of the nitrogenase molybdenum-iron (MoFe)-protein reveals novel structures for the FeMo-cofactor and P-cluster pair. These findings suggest new insights into substrate binding and redox reactions in nitrogen fixation.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinorganic Chemistry

Background:

  • The nitrogenase molybdenum-iron (MoFe)-protein is crucial for biological nitrogen fixation.
  • Understanding the precise structures of its catalytic centers, the FeMo-cofactor and P-cluster pair, is essential for elucidating enzyme mechanisms.

Purpose of the Study:

  • To crystallographically verify recently proposed structures of the FeMo-cofactor and P-cluster pair in Azotobacter vinelandii nitrogenase.
  • To investigate the coordination environments and potential functional implications of these metal centers.

Main Methods:

  • X-ray crystallography at 2.2 angstrom resolution.

Main Results:

  • Hexacoordinate sulfur atoms were not observed in either the FeMo-cofactor or P-cluster pair.

Related Experiment Videos

  • Iron atoms in the FeMo-cofactor exhibit trigonal coordination by nonprotein ligands, with potential iron-iron bonding interactions.
  • Two sulfurs in the P-cluster pair are closely associated, suggesting a disulfide bond formation.
  • A cavity was identified within the FeMo-cofactor, potentially involved in substrate binding.

    • Conclusions:

    • The verified structures challenge previous models and provide a refined understanding of the nitrogenase active site.
    • The observed structural features suggest a mechanism for substrate access and highlight the dynamic nature of the P-cluster sulfurs in redox processes.