title: The pH dependence of the reconstitution reaction of apotyrosinase: the question of Cu(I) versus Cu(II).
abstract: The rates of reconstitution of apotyrosinase by CuSO4 at various pH values have been determined. The rate at pH 6.0 is 130 times faster than that at pH 9.0. These results show that the idea of reconstitution by Cu(I) being a faster process than by Cu(II) by a factor of 200 should be discarded.
authors.affiliation: Ottawa-Carleton Chemistry Institute, Carleton University Campus, Ont., Canada.
authors.forename: D C
authors.initials: DC
authors.lastname: Wigfield
authors.forename: D M
authors.initials: DM
authors.lastname: Goltz
mesh_terms: D001051:Apoenzymes / Q000378:metabolism*; D001059:Apoproteins / Q000378:metabolism*; D004156:Catechol Oxidase / Q000378:metabolism*; D002704:Chlorates / Q000378:metabolism; D003300:Copper / Q000378:metabolism*; D019327:Copper Sulfate; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D014442:Monophenol Monooxygenase / Q000378:metabolism*; D009570:Nitriles / Q000378:metabolism*
chemical_list: D001051:Apoenzymes; D001059:Apoproteins; D002704:Chlorates; D009570:Nitriles; D003300:Copper; D004156:Catechol Oxidase; D014442:Monophenol Monooxygenase; D019327:Copper Sulfate