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Acid-assisted anion interaction with deoxyhemerythrin.

P C Wilkins, R G Wilkins

    Biochimica Et Biophysica Acta
    |March 18, 1987
    PubMed
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    Anions like azide (N3-), cyanate (CNO-), and fluoride (F-) bind to deoxyhemerythrin, forming stable adducts. A proton is essential for this binding, even at high pH, contributing to the protein

    Area of Science:

    • Biochemistry
    • Protein-ligand interactions
    • Bioinorganic chemistry

    Background:

    • Deoxyhemerythrin is an oxygen-transporting protein.
    • Understanding anion binding is crucial for elucidating hemerythrin's function and mechanism.
    • Previous studies have not fully characterized the thermodynamic and kinetic aspects of specific anion interactions.

    Purpose of the Study:

    • To investigate the interaction of azide (N3-), cyanate (CNO-), and fluoride (F-) with deoxyhemerythrin.
    • To determine the thermodynamic and kinetic parameters governing these anion bindings.
    • To elucidate the role of protons in adduct formation and the stability of the resulting complexes.

    Main Methods:

    • Competition assays with oxygen (O2) were employed to monitor anion binding.

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  • Experiments were conducted across a pH range of 6 to 9 and temperatures from 3°C to 25°C.
  • Ionic strength was maintained at 0.5 M using sodium sulfate (Na2SO4).

    • Main Results:

    • A proton is integral to adduct formation, remaining bound to the protein even at pH 9.
    • Thermodynamic and kinetic parameters for N3-, CNO-, and F- interactions were quantified.
    • The formed adducts exhibit significant stability, with dissociation half-lives from 7 s (N3-) to 70 s (CNO-, F-) at 25°C.

    Conclusions:

    • The binding of N3-, CNO-, and F- to deoxyhemerythrin involves protonation, likely of a bridged hydroxy group.
    • The observed stability of the anion-deoxyhemerythrin adducts suggests a mechanism involving protonation or bridge-breakage.
    • These findings provide insights into the structural and functional properties of hemerythrin and its anion-binding capabilities.