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Related Experiment Videos

Redox-dependent structural changes in the nitrogenase P-cluster

J W Peters1, M H Stowell, S M Soltis

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

Biochemistry
|February 11, 1997
PubMed
Summary
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The nitrogenase MoFe-protein

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Nitrogenase is a key enzyme responsible for biological nitrogen fixation.
  • The MoFe-protein component contains the P-cluster, crucial for enzyme activity.
  • Understanding P-cluster structure is vital for comprehending nitrogenase function.

Purpose of the Study:

  • To determine the high-resolution structures of the nitrogenase MoFe-protein in two distinct redox states.
  • To elucidate the structural basis of P-cluster interconversion during redox changes.
  • To investigate the role of the P-cluster in electron and proton transfer.

Main Methods:

  • X-ray crystallography at 2.0 A resolution.
  • Electron Paramagnetic Resonance (EPR) spectroscopy on protein crystals.

Related Experiment Videos

  • Structural refinement and comparative analysis of two enzyme oxidation states.

    • Main Results:

    • The P-cluster contains 8Fe and 7S atoms in both oxidized and reduced states.
    • Redox interconversion involves movement of two Fe atoms and altered protein coordination.
    • The P-cluster structure differs between the oxidized (P(OX)) and native/reduced (P(N)) states.
    • A revised model for the P-cluster structure is proposed, differing from the 8Fe-8S model.

    Conclusions:

    • Redox-dependent structural changes in the P-cluster are identified.
    • These structural dynamics suggest a role for the P-cluster in coupling electron and proton transfer.
    • The findings refine our understanding of the mechanism of nitrogen fixation.