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Related Experiment Videos

On the evolution of blue proteins.

L Ryden, J O Lundgren

    Biochimie
    |January 1, 1979
    PubMed
    Summary

    This study suggests that plastocyanins, azurins, and related blue copper proteins share a common ancestor. Evolutionary analysis reveals distinct divergence paths for these proteins, including duplication in ceruloplasmin.

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    Area of Science:

    • Biochemistry
    • Molecular Evolution
    • Bioinorganic Chemistry

    Background:

    • Blue copper proteins, including plastocyanins and azurins, are crucial electron transfer agents.
    • Human ceruloplasmin and bovine mitochondrial cytochrome c oxidase subunit II are also implicated in copper binding and redox functions.

    Purpose of the Study:

    • To investigate the evolutionary relationships among various blue copper-binding proteins.
    • To determine if these proteins share a common evolutionary origin (monophyly).

    Main Methods:

    • Comparative analysis of amino acid sequences using statistical methods.
    • Construction of a most parsimonious phylogenetic tree.

    Main Results:

    • Evidence suggests all examined blue copper proteins are monophyletic.
    • Human ceruloplasmin sequences indicate a gene duplication event.
    • Phylogenetic analysis points to the azurin and plastocyanin ancestor as the earliest divergence.

    Conclusions:

    • Plastocyanins, azurins, stellacyanin, ceruloplasmin, and cytochrome c oxidase subunit II likely evolved from a common ancestral protein.
    • Stellacyanin and ceruloplasmin evolved from the plastocyanin lineage.
    • Cytochrome c oxidase subunit II evolved from the azurin lineage.

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