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Selenium binding to beef-kidney rhodanese.

C Cannella, L Pecci, A Finazzi Agro

    European Journal of Biochemistry
    |June 16, 1975
    PubMed
    Summary
    This summary is machine-generated.

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    Beef kidney rhodanese reacts with selenosulfate, forming a unique sulfoselenide group. This selenium-enzyme intermediate is identified as a cysteinyl-selenium derivative, offering insights into sulfur-selenium biochemistry.

    Area of Science:

    • Biochemistry
    • Enzymology
    • Bioinorganic Chemistry

    Background:

    • Rhodanese is a key enzyme involved in sulfur metabolism.
    • The interaction of enzymes with selenium compounds is of significant biochemical interest.
    • Understanding enzyme-sulfur-selenium interactions can elucidate novel biochemical pathways.

    Purpose of the Study:

    • To investigate the reaction mechanism between beef kidney rhodanese and selenosulfate.
    • To characterize the resulting selenium-enzyme intermediate.
    • To elucidate the nature of the selenium binding to rhodanese.

    Main Methods:

    • Spectroscopic analysis (UV-Vis absorption) to detect spectral changes.
    • Enzyme kinetics and fluorescence spectroscopy to study enzyme activity and binding.

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  • Chemical treatments with cyanide, sulfite, selenite, and glutathione to probe the intermediate.
  • Comparison with model complexes to identify the selenium-rhodanese adduct.

    • Main Results:

    • Selenium treatment of rhodanese produced a characteristic absorption maximum at 375 nm, indicative of a sulfoselenide group.
    • This spectral feature was reversible upon cyanide addition, yielding selenocyanate.
    • Enzyme fluorescence was quenched by selenosulfate, with recovery observed upon treatment with cyanide or sulfite, but not selenite or glutathione.
    • Spectroscopic and chemical evidence identified the selenium-rhodanese intermediate as a cysteinyl-selenium derivative.

    Conclusions:

    • Beef kidney rhodanese reacts with selenosulfate to form a stable sulfoselenide intermediate.
    • The selenium moiety is covalently bound to a cysteine residue within the rhodanese active site.
    • This study provides a detailed characterization of a novel sulfur-selenium enzyme adduct, advancing the understanding of selenium biochemistry.