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Título: | An ionizable active-site tryptophan imparts catalase activity to a peroxidase core |
Autor: | Loewen, Peter C.; Carpena, Xavi CSIC ORCID; Vidossich, Pietro; Fita, Ignacio CSIC ORCID ; Rovira, Carme | Fecha de publicación: | 2-may-2014 | Editor: | American Chemical Society | Citación: | Journal of the American Chemical Society 136(20): 7249-7252 (2014) | Resumen: | Catalase peroxidases (KatGs) are bifunctional heme proteins that can disproportionate hydrogen peroxide (catalatic reaction) despite their structural dissimilarity with monofunctional catalases. Using X-ray crystallography and QM/MM calculations, we demonstrate that the catalatic reaction of KatGs involves deprotonation of the active-site Trp, which plays a role similar to that of the distal His in monofunctional catalases. The interaction of a nearby mobile arginine with the distal Met-Tyr-Trp essential adduct (in/out) acts as an electronic switch, triggering deprotonation of the adduct Trp. © 2014 American Chemical Society. | Versión del editor: | http://dx.doi.org/10.1021/ja502794e | URI: | http://hdl.handle.net/10261/111012 | DOI: | 10.1021/ja502794e | Identificadores: | doi: 10.1021/ja502794e issn: 1520-5126 |
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