Abstract
IT was thought that, analogously to the iron in hæmoglobin, the copper of hæmocyanin remained in the cuprous (Cu+) state when the pigment took up oxygen1. This was questioned2 because the characteristic blue colour of the cupric ion (Cu++) appeared when oxyhæmocyanin was formed, as well as on other grounds. It has since been shown3, using the hæmocyanin of Busycon, Loligo, Homarus and Limulus, that in fact half the copper becomes Cu++ and the rest remains Cu+. There was occasion to confirm this on the bloods of Helix and Maia, in the course of other work4. Klotz and Klotz3 showed that the oxygenation probably depends on the co-operation of the two ions. A number of further differences in properties between hæmocyanin and hæmoglobin also were explained by their important discovery.
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References
Dawson, C. R., and Malette, M. F., “Adv. Protein Chem.”, 2, 179 (1945).
Schulman, M. P., and Wald, G., Biol. Bull. Woods Hole, 101, 239 (1951).
Klotz, I. M., and Klotz, T. A., Science, 121, 477 (1955).
Needham, A. E., Comp. Biochem. Physiol., 1, 72 (1960).
Conant, J. B., et al., J. Biol. Chem., 101, 463 (1933).
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NEEDHAM, A. The Problem of ‘Methæmocyanin’. Nature 189, 308–309 (1961). https://doi.org/10.1038/189308a0
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DOI: https://doi.org/10.1038/189308a0
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