TY  - JOUR
PY  - 2010//
TI  - Studies of the competing rates of catechol oxidation and suicide inactivation of tyrosinase
JO  - Arkivoc
A1  - Ramsden, C.A.
A1  - Riley, P.A.
SP  - 248
EP  - 254
VL  - 2010
IS  - 10
N2  - 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.<p /> <p>Language: en</p>
LA  - en
SN  - 1551-7012
UR  - http://dx.doi.org/10.3998/ark.5550190.0011.a20
ID  - ref1
ER  -