Skip to main content
SpringerLink
Log in

Biliverdin as an electron transfer catalyst for superoxide ion in aqueous medium

  • Short Communications
  • Published:
Experientia Aims and scope Submit manuscript

    We’re sorry, something doesn't seem to be working properly.

    Please try refreshing the page. If that doesn't work, please contact support so we can address the problem.

Summary

Stopped flow experiments gave evidence of the formation of a biliverdin-superoxide complex and/or a biliverdin radical anion by reaction of aqueous O2 − with biliverdin. Such transient species are likely intermediates both in the bleaching of biliverdin, during exposure to the aerobic xanthine oxidase reaction, and in the reduction of ferricytochromec under the same conditions.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

References

  1. Biliverdin plays a key role in the catabolism of heme in that it is formed in vivo as the first isolable product of the oxidative break-down of the protoporphyrin ring: see Schmid, R., and McDonagh, A. F., in: The Porphyrins, vol. 6, p. 257. Ed. D. Dolphin, Academic Press, New York 1979.

    Chapter  Google Scholar 

  2. Robertson, P. Jr and Fridovich, I., Archs Biochem. Biophys.213 (1982) 353.

    Article  CAS  Google Scholar 

  3. Galliani, G., Monti, D., Speranza, G., and Manitto, P., Tetrahedron Lett.25 (1984) 6037.

    Article  CAS  Google Scholar 

  4. Fridovich, I., J. biol. Chem.245 (1970) 4053.

    Article  CAS  PubMed  Google Scholar 

  5. Sawyer, D. T., and Valentine, J. S., Acc. Chem. Res.14 (1981) 393.

    Article  CAS  Google Scholar 

  6. Manitto, P., and Monti, D., Experientia35 (1979) 9.

    Article  CAS  Google Scholar 

  7. Land, E. J., Sloper, R. W., and Truscott, T. G., Radiation Res.96 (1983) 450.

    Article  CAS  PubMed  Google Scholar 

  8. Both CO2H groups of BV are likely dissociated under the reaction condition (pH 7.62). See McDonagh, A. F., in: The Porphyrins, vol. 6, p. 293. Ed. D. Dolphin. Academic Press, New York 1979.

    Book  Google Scholar 

  9. This could explain some kinetic discrepancies observed by Fridovich using cytochromec, instead of superoxide dismutase, as a competitor of BV for O2 −(see Robertson Jr and Fridovich2).

    Article  CAS  Google Scholar 

  10. Ferguson-Miller, S., Brautigan, D. L., and Margoliash, E., in: The Porphyrins, vol. 7, p. 200. Ed. D. Dolphin. Academic Press, New York 1979.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Dipartimento di Chimica Organica e Industriale dell'Università and Centro di Studio per le Sostanze Organiche Naturali del CNR, Via Venezian 21, I-20133, Milano, Italy

    G. Galliani, D. Monti, G. Speranza & P. Manitto

  2. Centro Studi Maria Branca, Via E. Porro 1, I-20158, Milano, Italy

    G. Galliani, D. Monti, G. Speranza & P. Manitto

Authors
  1. G. Galliani
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. D. Monti
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. G. Speranza
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. P. Manitto
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Galliani, G., Monti, D., Speranza, G. et al. Biliverdin as an electron transfer catalyst for superoxide ion in aqueous medium. Experientia 41, 1559–1560 (1985). https://doi.org/10.1007/BF01964806

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01964806

Key words

Search

Navigation