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Dioxygen replacement reaction in myoglobin.

D Beece, L Eisenstein, H Frauenfelder

    Biochemistry
    |July 24, 1979
    PubMed
    Summary
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    Researchers studied myoglobin

    Area of Science:

    • Biophysics
    • Biochemistry
    • Physical Chemistry

    Background:

    • Myoglobin (Mb) is a protein crucial for oxygen transport.
    • Understanding ligand binding and dissociation kinetics is vital for protein function.
    • The reaction MbCO + O2 <=> MbO2 + CO involves complex dynamics within the protein environment.

    Purpose of the Study:

    • To investigate the replacement reaction of carbon monoxide (CO) by oxygen (O2) in myoglobin.
    • To determine the oxygen dissociation rate (kO2) from myoglobin across a wide temperature range.
    • To elucidate the mechanisms of ligand escape and rebinding within the myoglobin protein structure.

    Main Methods:

    • Flash photolysis was employed to initiate the CO dissociation from myoglobin.
    • Kinetic measurements were performed over a broad temperature range (140–320 K) and time scale (2 µs–200 s).

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  • The study analyzed CO rebinding kinetics in the presence and absence of oxygen, and O2 replacement by CO.

    • Main Results:

    • Two distinct pathways were observed: CO rebinding within the protein and CO migration into the solvent.
    • Rebinding rates were independent of oxygen presence when CO remained within the protein.
    • The rate of O2 replacement by CO allowed for the calculation of the oxygen dissociation rate (kO2) between 260–320 K.

    Conclusions:

    • The experimental data support a multi-barrier model for ligand binding and dissociation in myoglobin.
    • Protein dynamics play a significant role in modulating ligand escape and rebinding.
    • The determined oxygen dissociation rates provide insights into myoglobin's oxygen transport efficiency.