Citation

Ramsden CA, Riley PA. Arkivoc 2010; 2010(10): 248-254.

Copyright

(Copyright © 2010)

DOI

10.3998/ark.5550190.0011.a20

PMID

unavailable

Abstract

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 structure-rate 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). © ARKAT USA, Inc.

Language: en

Keywords

Regression analysis; Tyrosinase; Catechols; Suicide-inactivation; Oxidation rates