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State of Copper in Polyphenoloxidase (Tyrosinase)

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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

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  2. Keilin, D., and Mann, T., Proc. Roy. Soc., B, 125, 187 (1938).

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Authors and Affiliations

  1. Research Department, Istituto Regina Elena per lo Studio e la Cura dei Tumori, Rome

    DENIS KERTÉSZ

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  1. DENIS KERTÉSZ
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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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