Dye-decolorizing peroxidases (DyPs) represent the most recently classified hydrogen peroxide–dependent heme peroxidase family. Here, we present the high-resolution crystal structures of WT B-class DyP from the pathogenic bacterium Klebsiella pneumoniae (KpDyP) (1.6A˚ ) and the variants D143A (1.3 A˚ ), R232A (1.9 A˚ ), and D143A/R232A (1.1 A˚ ). We demonstrate the impact of elimination of the DyP-typical, distal residues Asp-143 and Arg-232 on (i) the spectral and redox properties, (ii) the kinetics of heterolytic cleavage of hydrogen peroxide, (iii) the formation of the low-spin cyanide complex, and (iv) the stability and reactivity of an oxoiron(IV)porphyrin-cation radical (Compound I).
Roles of the distal Asp-Arg pair in Compound I formation of K. pneumoniae dye-decolorizing peroxidase / Pfanzagl, Vera; Hofbauer, Stefan; Nys, Kevin; Djinovic-Carugo, Kristina; Battistuzzi, Gianantonio; Van Doorslaer, Sabine; Furtmuller, Paul G.; Obinger, Christian. - In: JBIC. - ISSN 0949-8257. - 22:(2018), pp. S130-S130. (Intervento presentato al convegno 18th International Conference on Biological Inorganic Chemistry (ICBIC) tenutosi a Florianopolis, BRAZIL nel JUL 31-AUG 04, 2017).
Roles of the distal Asp-Arg pair in Compound I formation of K. pneumoniae dye-decolorizing peroxidase
Gianantonio Battistuzzi;
2018
Abstract
Dye-decolorizing peroxidases (DyPs) represent the most recently classified hydrogen peroxide–dependent heme peroxidase family. Here, we present the high-resolution crystal structures of WT B-class DyP from the pathogenic bacterium Klebsiella pneumoniae (KpDyP) (1.6A˚ ) and the variants D143A (1.3 A˚ ), R232A (1.9 A˚ ), and D143A/R232A (1.1 A˚ ). We demonstrate the impact of elimination of the DyP-typical, distal residues Asp-143 and Arg-232 on (i) the spectral and redox properties, (ii) the kinetics of heterolytic cleavage of hydrogen peroxide, (iii) the formation of the low-spin cyanide complex, and (iv) the stability and reactivity of an oxoiron(IV)porphyrin-cation radical (Compound I).
Pubblicazioni consigliate
I metadati presenti in IRIS UNIMORE sono rilasciati con licenza Creative Commons CC0 1.0 Universal, mentre i file delle pubblicazioni sono rilasciati con licenza Attribuzione 4.0 Internazionale (CC BY 4.0), salvo diversa indicazione.
In caso di violazione di copyright, contattare Supporto Iris
