Abstract
THE transformation of oxyhaemoglobin (HbO2) to methaemoglobin (Hb+) involves an electron transfer whereby the ferrous haem iron is oxidized, with the simultaneous reduction of the oxidant, oxygen. In the event of the O2 being fully reduced (to H2O) in the process1, 1 mole of HbO2 will be expected to release 0.75 mole of O2, for an electron donated by the ferrous iron can reduce only a quarter of the oxygen released by the iron in going to the trivalent state. In a study of the conversion of oxymyoglobin to metmyoglobin, however, George and Stratmann2 have reported the consumption of 2.5 moles of O2 for each mole of haem iron oxidized and attributed the excess to unspecified electron donor groups in the protein moiety.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Keilin, D., Nature, 191, 769 (1961).
George, P., and Stratmann, C. J., Biochem. J., 51, 103 (1952).
Brill, A. S., and Williams, R. J. P., Biochem. J., 78, 253 (1961).
Badger, R. M., Wright, A. C., and Whitlock, J., J. Chem. Phys., 43, 4345 (1963).
Weil, L., Arch. Biochem. Biophys., 110, 57 (1965).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
POSSANI, L., BANERJEE, R., BALNY, C. et al. Oxidation of Haemoglobin by Oxygen in Light: Possible Role of Singlet Oxygen. Nature 226, 861–862 (1970). https://doi.org/10.1038/226861a0
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1038/226861a0
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.
