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Related Experiment Videos

Reaction of hemerythrin with disulfides.

P C Harrington, R G Wilkins

    Biochemistry
    |January 1, 1985
    PubMed
    Summary

    Hemerythrin

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    Kinetics and thermodynamics of the reaction of deoxyhemerythrin with nitric oxide.

    Acta chemica Scandinavica (Copenhagen, Denmark : 1989)·1989

    Area of Science:

    • Biochemistry
    • Protein Chemistry

    Background:

    • Hemerythrin is an oxygen-binding protein found in marine invertebrates.
    • Understanding hemerythrin's structure-function relationship is crucial for studying oxygen transport mechanisms.

    Purpose of the Study:

    • To investigate the reaction kinetics of hemerythrin from Phascolopsis gouldii with sulfhydryl reagents.
    • To elucidate the role of cysteine residues in hemerythrin structure and function.

    Main Methods:

    • Spectrophotometric analysis of hemerythrin reactions with specific disulfide reagents.
    • Kinetic studies under varying conditions (pH, ion presence).

    Main Results:

    • One mole of disulfide reacted per hemerythrin subunit, indicating a single reactive cysteine at residue 50.
    • Reaction caused dissociation of the octameric protein into monomers.
    • First-order rate constants were determined for methemerythrin and metazidohemerythrin.
    • Perchlorate ion inhibited methemerythrin reactions but not metazidohemerythrin reactions.

    Conclusions:

    • The observed first-order kinetics suggest a protein conformational change controls the reaction rate.
    • This conformational change appears to be a dominant factor in several hemerythrin reactions.
    • The findings provide insights into hemerythrin's structural dynamics and reactivity.

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