Abstract
This chapter focuses on the role of flavins in hydroxylase reactions. The mechanism of hydroxylation has been investigated using two enzyme systems, p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens and melilotate hydroxylase from Pseudomonas spp., as well as two model systems. A comparison of the rate of reduction of the enzyme flavin in the presence and absence of melilotate is shown. The analogues which have been investigated simulated many of the characteristics of p-hydroxybenzoate, such as spectral perturbations on binding, but none of the previously investigated analogues mimic the effector role. The data may be compared to the fluorescence titration of p-hydroxybenzoate hydroxylase with p-hydroxybenzoate monitoring the quenching of flavin fluorescence upon formation of the enzyme-p-hydroxybenzoate complex. The nature of the active oxygen produced during the hydroxylation phase of the catalytic cycle is of great interest.
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