Activation parameters for the reconstitution of apotyrosinase by copper.
The reaction of apotyrosinase with divalent copper to give enzymatically active tyrosinase has been studied at pH 8.2 and temperatures from 278 to 303 K. At a 10-fold excess of Cu(II) over enzyme, the pseudo-first order rate constants range from 1.32 x 10(-3) s-1 to 2.93 x 10(-2) s-1 and yield activation parameters of delta H not equal to = 85 +/- 3 kJ.mol-1 and delta S not equal to = 5 +/- 20 J.mol-1.K-1. The near zero value for the entropy of activation is discussed.
Wigfield
D C
DC
Ottawa-Carleton Chemistry Institute, Department of Chemistry, Carleton University, Ont., Canada.
Goltz
D M
DM
D001051:Apoenzymes / Q000378:metabolism*; D003300:Copper / Q000378:metabolism*; D004789:Enzyme Activation; D014442:Monophenol Monooxygenase / Q000378:metabolism*; D013816:Thermodynamics
D001051:Apoenzymes; D003300:Copper; D014442:Monophenol Monooxygenase