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Microsecond luminescence emission from copper cytochrome c.

P Glatz, B Chance, J M Vanderkooi

    Biochemistry
    |August 7, 1979
    PubMed
    Summary
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    Copper-substituted cytochrome c luminescence reveals temperature-dependent decay and spectral shifts below 80 K. Its interaction with mitochondrial binding sites depends on cytochrome c's electronic state.

    Area of Science:

    • Biochemistry
    • Biophysics
    • Spectroscopy

    Background:

    • Cytochrome c is a crucial protein in cellular respiration and electron transport.
    • Understanding its electronic and dynamic properties is key to elucidating mitochondrial function.
    • Luminescence spectroscopy offers a sensitive probe for studying protein dynamics and interactions.

    Purpose of the Study:

    • To investigate the temperature-dependent luminescence properties of copper-substituted cytochrome c.
    • To determine intramolecular rate parameters by comparing with metal-substituted porphyrins.
    • To explore the interaction of copper-substituted cytochrome c with mitochondrial components.

    Main Methods:

    • Low-temperature luminescence spectroscopy (below 80 K).
    • Kinetic analysis of triplet and quartet decay times.

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  • Comparative analysis with metal-substituted porphyrins.
  • Investigation of luminescence changes upon binding to mitochondria and cytochrome c oxidase.

    • Main Results:

    • Observed temperature-dependent luminescence decay modes and spectral shifts below 80 K.
    • Determined intramolecular rate parameters, including triplet decay time (13 ± 1 μs at 77 K) and quartet decay time (12 ± 5 μs below 30 K).
    • Demonstrated alterations in luminescence intensity and decay time upon binding of Cu cytochrome c to mitochondria and cytochrome c oxidase.

    Conclusions:

    • The luminescence properties of Cu-substituted cytochrome c are sensitive to temperature and its electronic state.
    • Intramolecular dynamics can be characterized using luminescence decay kinetics.
    • Evidence suggests a specific interaction between cytochrome c and its mitochondrial binding site, influenced by the protein's electronic configuration.