Substrate analog binding to the coupled binuclear copper active site in tyrosinase

Stopped-flow Fluorescence Studies of Inhibitor Binding to Tyrosinase from Streptomyces antibioticus

“…The stable percentage of Ty met in resting preparations may reflect a natural equilibrium between the three Ty species present in solution. Establishment of this equilibrium may be connected with the dissociation of peroxide from Ty oxy resulting in the formation of Ty met , as observed for N. crassa Ty (45). This would be consistent with the observed slow decay of Ty oxy to Ty met in fresh preparations of S. antibioticus Ty red .…”

Substrate-dependent kinetics in tyrosinase-based biosensing: amperometry vs. spectrophotometry

“…For example, the Rgroup of phenols influences the reaction rate of tyrosinase via two factors, namely, the electronegativity of the R-group and the steric hindrance caused by the size of this group. The reactivity of tyrosinase decreases upon a transition of the substituent in the para position of phenols from electron donating to electron withdrawing [26], and tyrosinase does not react with bulky phenols [27]. There are few studies on kinetics of tyrosinase for different phenolic substrates with alkyl groups side chain such as methyl- [28], ethyl- [29], and tert-butylphenol [30].…”

The o‐diphenol oxidase activity of arthropod hemocyanin

“…The transient adduct is suited either to chemical attack at the o-position (monophenolase activity) and/or to electron transfer involving the metal (catecholase activity) [1,2,10].…”