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The involvement of superoxide anions in the autoxidation of various cofactors of cysteamine-oxygenase

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Summary

The reduction of tetranitroblue tetrazolium with cysteamine, mediated by a number of dyes, elemental sulphur, elemental selenium and selenide, under aerobic conditions,was inhibited to various extent upon addition of superoxide dismutase.

A strict parallelism between the ability to produce O -2 ions and the property of those compounds to act as cofactors for cysteamine-oxygenase, to yield hypotaurine, has been observed. Based on the fact that the autoxidation of cysteamine also gives rise to O -2 formation, though to a minor extent, we propose a mechanism for cysteamine-oxygenase action. This mechanism was derived from the data obtained in the model system studied.

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Authors and Affiliations

  1. Institute of Biological Chemistry, University of Rome, Rome, Italy

    Silvestro Dupré, Giorgio Federici, Luigi Santoro, Maria Rosaria Rossi Fanelli & Doriano Cavallini

Authors
  1. Silvestro Dupré
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  2. Giorgio Federici
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  3. Luigi Santoro
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  4. Maria Rosaria Rossi Fanelli
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  5. Doriano Cavallini
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Additional information

This work is part of a program supported by a grant from the Consiglio Nazionale delle Ricerche. Part of the experimental data presented in this paper, including the detection of O -2 ions during the autoxidation of cysteamine and cysteine, has been presented on the 9th International Congress of Biochemistry held in Stockholm, July 1973.

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Dupré, S., Federici, G., Santoro, L. et al. The involvement of superoxide anions in the autoxidation of various cofactors of cysteamine-oxygenase. Mol Cell Biochem 9, 149–154 (1975). https://doi.org/10.1007/BF01751310

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  • DOI: https://doi.org/10.1007/BF01751310

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