Structure and function of intermediates involved in metalloenzymatic N-oygenation and oxidation reactions

This award in the Chemistry of Life Processes (CLP) program supports work by Professors J. Martin Bollinger, Jr. and Carsten Krebs at the Pennsylvania State University to study the structure and reactivity of the enzyme AurF from Streptomyces thioluteus. This enzyme is involved in the biosynthesis of the antibiotic aureothin and catalyzes the oxidation of para-aminobenzoate to para-nitrobenzoate. It employs a stable peroxo-diiron(III/III) intermediate as the oxidant. The unusual stability of the intermediate will permit determination of the intermediate's structure by a combination of crystallographic, spectroscopic, and computational methods. By defining the intermediate's reactivity toward substrate analogues, the team will unravel the mechanism of the reaction.

Peroxo-diiron(III/III) complexes are common to a number of important biological oxidations that use dioxygen directly as the oxidant. New catalysts can be designed that mimic the structures and reactivities of these complexes.