Estabrook and coworkers have developed an enzymatic analysis for the oxidation of catechol depicted in Figure 1b. The rate of this oxidation (k2) is so high that the

[Figure 1.]

rate of the O-dealkylation reactions of monocatechol ethers (k1) may perhaps be conveniently followed by monitoring catechol concentrations as it is produced. That is with k2 >> k1, a combined dealkylation and oxidation enzymatic system might be developed to provide kinetic data on step 1, ie. on k1 values.

With this in mind, a series of appropriate substrates ie. O-monoalkyl catechol ethers needed to be prepared. That part of the overall scheme is the focus of the present work and was achieved as outlined in Figure 2.

[Figure 2.]

Synthetically the yields of n-alkyl mono- and diethers levelled off at about 70%. Conditions were developed (by changing base to halide ratios, etc.) so as to optimize selectively the yields of mono- or diether. The evidence accumulated suggests that the monoethers were the precursors of the dialkylated products.

With the isopropyl compound the overall yields were much poorer (~20%), this being due to the ease with which the parent halide undergoes elimination under the reaction conditions. A surprising anomaly was the fact that with n-octyl bromide as reagent diether formation occurred exclusively under the present range of conditions.

Physical data (1H-NMR and IR) verified the structures of the compounds prepared. In general the various structural parameters e.g. the position of […] for the OH group in 1H-NMR, were insensitive to the nature of the alkyl group. This was also true for the pKa values for the series of monoalkyl catechol ethers.

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F. L. Scott

Advisor/Committee Member

T. C. Morrill


Physical copy available from RIT's Wallace Library at QA305.E7 D48 1983


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