Abstract
IT was shown in the classical work of Kubowitz1 and of Keilin and Mann2 that the prosthetic group of polyphenoloxidase is constituted by copper. Since then it has been unanimously admitted that the metal of the enzyme is in the bivalent state and that the catalytic activity of the enzyme is based on the change of valency cupric ⇌ cuprous, as follows (for excellent discussions, see refs. 3,4): 
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References
Kubowitz, F., Biochem. Z., 299, 32 (1938).
Keilin, D., and Mann, T., Proc. Roy. Soc., B, 125, 187 (1938).
Singer, T. P., and Kearney, E. B., in “The Proteins”, 2, 135 (edit. by Neurath, H., and Bailey, K., Acad. Press, New York, 1954).
Hoffmann-Ostenhof, O., “Enzymologie”, 557 (Springer Verlag, Wien, 1954).
Kertész, D., and Zito, R., Nature, 179, 1017 (1957).
Hoste, J., Anal. Chem. Acta, 4, 23 (1950).
Klotz, I. M., Urquart, J. M., and Fiess, H. A., J. Amer. Chem. Soc., 74, 5537 (1952). Warner, R. C., and Weber, I., ibid., 75, 5094 (1953).
Klotz, I. M., and Klotz, T. A., Science, 121, 477 ; 122, 559 (1955). Williams, R. J. P., ibid., 122, 558 (1955).
Warburg, O., Biochem. Z., 187, 255 (1927) ; “Heavy Metal Prosthetic Groups”, 41 and 147 (Clarendon Press, Oxford, 1949).
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KERTÉSZ, D. State of Copper in Polyphenoloxidase (Tyrosinase). Nature 180, 506–507 (1957). https://doi.org/10.1038/180506a0
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DOI: https://doi.org/10.1038/180506a0
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