Open AccessPhenol hydroxylase from yeast
Author(s) -
SEJLITZ Torsten,
NEUJAHR Halina Y.
Publication year - 1987
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1987.tb13705.x
Subject(s) - yeast , phenol , chemistry , food science , biochemistry , organic chemistry
The binding of phenol to phenol hydroxylase was studied by equilibrium dialysis, spectrophotometric titration and by steady‐state kinetics. A binding model with two identical, negatively cooperative, effector/substrate‐binding sites per enzyme dimer is proposed. The spectral perturbation caused by phenol and the kinetics of the overall reaction were analysed with relation to the enzyme‐phenol complexes of the binding model. The main part of the spectral perturbation as well as of the increase in NADPH oxidation rate was achieved by one molecule of phenol bound per enzyme dimer. The properties of different enzyme‐phenol complexes, in terms of spectral changes, hydroxylase activity, oxidase activity and substrate inhibition are discussed. A new purification procedure is described.