Inhibitor Binding to the Binuclear Active Site of Tyrosinase: Temperature, pH, and Solvent Deuterium Isotope Effects

Biochemistry ◽  
1994 ◽  
Vol 33 (19) ◽  
pp. 5739-5744 ◽  
Author(s):  
Jennifer S. Conrad ◽  
Sharon R. Dawso ◽  
Esmine R. Hubbard ◽  
Theresa E. Meyers ◽  
Kenneth G. Strothkamp
1979 ◽  
Vol 44 (1) ◽  
pp. 110-122 ◽  
Author(s):  
Jiří Velek ◽  
Bohumír Koutek ◽  
Milan Souček

Competitive hydration and isomerisation of the quinone methide I at 25 °C in an aqueous medium in the region of pH 2.4-13.0 was studied spectrophotometrically. The only reaction products in the studied range of pH are 4-hydroxybenzyl alcohol (II) and 4-hydroxystyrene (III). The form of the overall rate equation corresponds to a general acid-base catalysis. The mechanism of both reactions for three markedly separated pH regions is discussed on the basis of kinetic data and solvent deuterium effect.


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