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Related Experiment Videos

Evolutionary relationships among copper proteins containing coupled binuclear copper sites.

K Lerch1, U A Germann

  • 1Biochemisches Institut der Universität Zürich, Switzerland.

Progress in Clinical and Biological Research
|January 1, 1988
PubMed
Summary

Copper proteins like hemocyanins and tyrosinases share homologous regions, suggesting a common ancestor. This research explores the evolution of these vital copper-binding proteins and their structural relationships.

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Area of Science:

  • Biochemistry
  • Molecular Evolution
  • Structural Biology

Background:

  • Copper proteins play crucial roles in biological processes.
  • Coupled binuclear copper centers are found in various proteins, including hemocyanins and tyrosinases.
  • Understanding the evolutionary relationships of these proteins is key to deciphering their functions.

Purpose of the Study:

  • To compare amino acid sequences of diverse copper proteins with coupled binuclear copper centers.
  • To investigate the evolutionary origins and relationships between hemocyanins, tyrosinases, and multicopper oxidases.
  • To elucidate the conserved and variable ligand environments within these copper-binding sites.

Main Methods:

  • Comparative analysis of amino acid sequences from arthropod and mollusc hemocyanins, tyrosinases, human ceruloplasmin, and fungal laccases.

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  • Integration of data from X-ray crystallography of hemocyanin and preliminary X-ray structure analysis of ascorbate oxidase.

    • Main Results:

    • A highly homologous C-terminal region was identified in hemocyanins and tyrosinases, containing conserved histidine ligands for the Cu(B) site.
    • The ligand environment for the Cu(A) site exhibited significant variability across different species.
    • Structural similarities were observed in the C-terminal regions of human ceruloplasmin, fungal laccase, and ascorbate oxidase.

    Conclusions:

    • Hemocyanin and tyrosinase likely evolved from a common mononuclear copper protein ancestor.
    • Independent evolution led to distinct tyrosinase and arthropodan hemocyanin types from this ancestral protein.
    • Multicopper oxidases may have evolved from an ancestral copper protein capable of binding multiple metal centers.