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Related Experiment Videos

7-Iron ferredoxin revisited.

C D Stout1

  • 1Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, California 92037.

The Journal of Biological Chemistry
|July 5, 1988
PubMed
Summary
This summary is machine-generated.

The crystal structure of Azotobacter vinelandii 7Fe ferredoxin was redetermined, correcting previous errors. This study reveals a unique 3Fe-4Fe cluster arrangement and identifies two free sulfhydryls, impacting protein function understanding.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • X-ray Crystallography

Background:

  • Ferredoxins are crucial electron transport proteins.
  • Azotobacter vinelandii 7Fe ferredoxin's structure was previously reported with inaccuracies.

Purpose of the Study:

  • To redetermine the crystal structure of Azotobacter vinelandii 7Fe ferredoxin.
  • To clarify the protein's structural features and iron-sulfur cluster coordination.

Main Methods:

  • X-ray crystallography with area detector data to 2.7-A resolution.
  • Utilized a new derivative for structural analysis.
  • Maintained protein crystals at pH 8.0.

Main Results:

  • The previously reported structure was found to be erroneous.

Related Experiment Videos

  • Confirmed findings from an independent recent report.
  • Identified a 3Fe cluster coordinated by Cys8, 16, 49 and a 4Fe cluster by Cys20, 39, 42, 45.
  • Discovered two free sulfhydryls: Cys11 and Cys24, with Cys24 near the [4Fe-4S] cluster.

    • Conclusions:

    • The N-terminal half of the protein fold resembles 8Fe ferredoxin.
    • C-terminal residues enclose the core structure.
    • The presence and location of free sulfhydryls suggest roles in protein stability or redox activity.