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Related Experiment Videos

Emission spectra from copper proteins containing type-3 centres.

M Bacci, M G Baldecchi, P Fabeni

    Biophysical Chemistry
    |March 1, 1983
    PubMed
    Summary

    Copper proteins exhibit novel fluorescence linked to carboxyl groups. This finding suggests interactions between amino acid carboxyls and the active site in these metalloproteins.

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    Area of Science:

    • Biochemistry
    • Biophysics
    • Spectroscopy

    Background:

    • Copper proteins with type-3 centers, such as ceruloplasmin, tyrosinase, and hemocyanin, are crucial metalloproteins.
    • These proteins play vital roles in biological processes, and understanding their photophysical properties is essential.

    Purpose of the Study:

    • To investigate the luminescence properties of copper proteins with type-3 centers.
    • To explore the origin of fluorescence in these systems and its potential link to specific functional groups.

    Main Methods:

    • Excitation of aqueous copper protein solutions within their absorption bands (325-345 nm).
    • Analysis of luminescence spectra, emission peaks (415-445 nm), and decay times (≤10 ns).
    • Comparative studies using carboxylic acids, amino acids, copper(II) carboxylates, acetic anhydride, and polypeptides.

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    Main Results:

    • Copper proteins showed typical luminescence spectra with emission peaks at 415-445 nm and decay times under 10 ns.
    • Strong analogous fluorescence was observed in concentrated carboxylic acid and amino acid solutions, also absorbing around 330 nm.
    • Fluorescence was less intense in copper(II) carboxylate solutions and absent in solutions lacking free carboxyl groups.

    Conclusions:

    • A novel fluorescence phenomenon was observed in the studied copper proteins.
    • The fluorescence is tentatively attributed to interactions involving carboxyl groups of amino acids near the active site.
    • This finding provides insights into the photophysical behavior and structural features of type-3 copper proteins.