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Publication Abstract from PubMed

Enzymatic degradation of azo dyes begins with the reduction of the azo bond. In this paper we report the crystal structures of the native azoreductase from Pseudomonas putida MET94 (PpAzoR) (1.60 A), of PpAzoR in complex with the anthraquinone-2-sulfonate (1.50 A) and of PpAzoR in complex with Reactive Black 5 dye (1.90 A). 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. This article is protected by copyright. All rights reserved.

The Crystal Structure of Pseudomonas putida AzoR: the active site revisited.,Goncalves AM, Mendes S, de Sanctis D, Martins LO, Bento I FEBS J. 2013 Oct 16. doi: 10.1111/febs.12568. PMID:24127652^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.