The enzymatic degradation of azo dyes begins with the reduction of the azo bond. In this article, we report the crystal structures of the native azoreductase from PseudomonasputidaMET94 (PpAzoR) (1.60 angstrom), of PpAzoR in complex with anthraquinone-2-sulfonate (1.50 angstrom), and of PpAzoR in complex with Reactive Black5 dye (1.90 angstrom). These structures reveal the residues and subtle changes that accompany substrate binding and release. Such changes highlight the fine control of access to the catalytic site that is required by the ping-pong mechanism, and in turn the specificity offered by the enzyme towards different substrates. The topology surrounding the active site shows novel features of substrate recognition and binding that help to explain and differentiate the substrate specificity observed among different bacterial azoreductases.
|Publication status||Published - 1 Jan 2013|