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Tyrosinase oxidation of catechols to ortho-quinones is accompanied by suicide inactivation of the enzyme. The rates of these competing processes vary and depend on the nature of ring substituents. For a series of 4-substituted catechols the relationships between structure and reaction rates have been examined using multiple regression. Significant but different structurerate relationships were found for each process. The oxidation rate (k1) is greatest for short hydrophobic substituents; there is an optimum substituent hydrophobicity (π ~ 0.7) for the rate of inactivation (k2).

Studies of the competing rates of catechol oxidation and suicide inactivation of tyrosinase