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Related Experiment Videos

Active site structures of deoxyhemerythrin and oxyhemerythrin.

R E Stenkamp, L C Sieker, L H Jensen

    Proceedings of the National Academy of Sciences of the United States of America
    |February 1, 1985
    PubMed
    Summary
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    X-ray crystallography reveals hemerythrin

    Area of Science:

    • Biochemistry
    • Structural Biology
    • Biophysics

    Background:

    • Hemerythrin is a nonheme-iron protein crucial for oxygen transport.
    • Understanding its structure-function relationship is key to deciphering oxygen binding mechanisms.

    Purpose of the Study:

    • To elucidate the structural differences and iron coordination in various forms of hemerythrin using X-ray crystallography.
    • To identify the precise binding site of dioxygen in oxyhemerythrin.

    Main Methods:

    • X-ray crystallography at 3.9-Å and 2.2-Å resolutions.
    • Difference electron-density mapping between deoxy and methemerythrin forms.

    Main Results:

    • Small structural differences observed between deoxy and methemerythrin, with similar iron coordination (one pentacoordinate, one hexacoordinate iron).

    Related Experiment Videos

  • Iron atoms are slightly farther apart in the deoxy form.
  • Dioxygen binds to the pentacoordinate iron atom in oxyhemerythrin, a site also occupied by azide in azidomethemerythrin.

    • Conclusions:

    • The binuclear iron center in hemerythrin maintains a consistent coordination environment across different functional states.
    • Dioxygen and azide share a common binding site on the pentacoordinate iron atom, providing insights into the protein's active site.