2,5-dihydroxyacetanilide epoxidase from Streptomyces LL-C10037 (DHAE I)
catalyzes the epoxidation of hydroquinone 4, to form epoxyquinone 7. DHAE I has been
purified to homogeneity, with an overall purification factor greater than 23,000. N-terminal
and internal amino acid sequences have been obtained from the purified enzyme so
that the epoxidase gene...
The first part of this thesis describes a study of the
characteristics of oxidation of a 1:2 iron(III):thiolate system in
methanolic solution and in water. This system was investigated as a
potential analog for the cysteine- and cysteamine-dioxygenase catalyzed
0₂-oxidation of cysteine and cysteamine, respectively, to the
corresponding sulfinic acids....
A series of compounds, 7-8 and 20-25, were tested as competitive inhibitors of 2,5-dihydroxyacetanilide epoxidase I (DHAE I) and DHAE II. A Hammett plot was constructed for each enzyme to determine the effect of electron density on inhibition. DHAE I gave a linear, highly correlated plot (r²=0.91) that signifies the...