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Heme protein fluorescence versus pressure.

M C Marden, G Hui Bon Hoa, F Stetzkowski-Marden

    Biophysical Journal
    |March 1, 1986
    PubMed
    Summary
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    High pressure causes heme proteins like myoglobin to unfold, significantly increasing tryptophan fluorescence. This pressure-induced unfolding is pH-dependent and varies between different heme proteins.

    Area of Science:

    • Biophysics
    • Protein Chemistry
    • Spectroscopy

    Background:

    • Ferric heme proteins exhibit fluorescence primarily from tryptophan residues.
    • Heme groups typically quench tryptophan fluorescence through energy transfer.
    • Protein structure and dynamics influence fluorescence properties.

    Purpose of the Study:

    • To investigate the effect of high pressure on the fluorescence spectra of ferric heme proteins.
    • To use fluorescence as a probe for pressure-induced protein unfolding.
    • To explore the pH-dependence and reversibility of these high-pressure transitions.

    Main Methods:

    • Measurement of fluorescence excitation and emission spectra.
    • Application of hydrostatic pressure up to 6,000 bars.

    Related Experiment Videos

  • Utilizing tryptophan fluorescence at 330-340 nm as an indicator.

    • Main Results:

    • Fluorescence intensity increases significantly at high pressures, indicating protein unfolding.
    • The pressure-induced unfolding is pH-dependent, with different transition midpoints and reversibility.
    • Sperm whale myoglobin, Aplysia myoglobin, leghemoglobin, and cytochrome P450 all exhibit distinct high-pressure fluorescence changes.

    Conclusions:

    • High pressure induces conformational changes in heme proteins, leading to increased tryptophan fluorescence.
    • The observed transitions are sensitive to pH and protein type, suggesting multiple high-pressure states.
    • Fluorescence measurements provide a method to estimate changes in the tryptophan-heme distance during unfolding.