The mechanism of action of tyrosinase on monophenols is complex, several processes
overlap in time, such as the hydroxylation of monophenols to o-diphenols, the oxidation of …

We study the suicide inactivation of tyrosinase acting on o-aminophenols and aromatic o-
diamines and compare the results with those obtained for the corresponding o-diphenols …

Tyrosinase shows a lag period in its action on monophenols (l-tyrosine). We propose an
approximate analytical solution for the lag period, which fulfils the dependences with regard …

A study of the monophenolase activity of tyrosinase by measuring the steady state rate with
a group of p-substituted monophenols provides the following kinetic information: kcatm and …

The complex reaction mechanism of tyrosinase involves three enzymatic forms, two
overlapping catalytic cycles and a dead-end complex. The deoxytyrosinase form binds …

The suicide inactivation mechanism of tyrosinase acting on its substrates has been studied.
The kinetic analysis of the proposed mechanism during the transition phase provides explicit …

A study of the diphenolase, o-aminophenol oxidase, and the aromatic o-diamine oxidase
activities of tyrosinase carried out by measuring the catalysis and suicide inactivation …

Deoxyarbutin, a potent inhibitor of tyrosinase, could act as substrate of the enzyme.
Oxytyrosinase is able to hydroxylate deoxyarbutin and finishes the catalytic cycle by …

The suicide inactivation mechanism of tyrosinase acting on its phenolic substrates has been
studied. Kinetic analysis of the proposed mechanism during the transition phase provides …

The stoichiometry of oxygen consumption during tyrosinase-catalyzed oxidation of an o-
diphenol (4-tert-butylcatechol, TBC) and a monophenol (4-tert-butylphenol, TBP) has been …