Here, for the first time, an ancestral bacterial heme peroxidase has been cloned and purified. It is shown to catalyse (besides conventional peroxidase activity) bromide and chloride oxidation more efficiently than LPO and MPO. The structure-function relationships of this new peroxidase in relation to its mammalian counterparts and its putative physiological role are discussed.
New highly stable chlorinating bacterial peroxidase with autocatalytically formed covalent heme to protein bonds / P. G., Furtmuller; M., Auer; C., Gruber; K., Pirker; D., Krioss; S., Hofbauer; M., Soudi; C., Obinger; M., Zamocky; Bellei, Marzia; Battistuzzi, Gianantonio. - In: JBIC. - ISSN 0949-8257. - STAMPA. - 19:(2014), pp. S281-S281. (Intervento presentato al convegno 16th International Conference on Biological Inorganic Chemistry (ICBIC) tenutosi a Grenoble, FRANCE nel JULY 22-26, 2013).
New highly stable chlorinating bacterial peroxidase with autocatalytically formed covalent heme to protein bonds
BELLEI, Marzia;BATTISTUZZI, Gianantonio
2014
Abstract
Here, for the first time, an ancestral bacterial heme peroxidase has been cloned and purified. It is shown to catalyse (besides conventional peroxidase activity) bromide and chloride oxidation more efficiently than LPO and MPO. The structure-function relationships of this new peroxidase in relation to its mammalian counterparts and its putative physiological role are discussed.
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