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Selected Publication:

Furtmüller, PG; Arnhold, J; Jantschko, W; Zederbauer, M; Jakopitsch, C; Obinger, C.
(2005): Standard reduction potentials of all couples of the peroxidase cycle of lactoperoxidase.
J Inorg Biochem. 2005; 99(5):1220-1229 FullText FullText_BOKU

Abstract:
Lactoperoxidase (LPO) is found in mucosal surfaces and exocrine secretions including milk, tears and saliva and has physiological significance in antimicrobial defense. Its predominant physiological role is to convert hydrogen peroxide and thiocyanate in hypothiocyanite. In this study, the standard reduction potentials of all redox couples involved in the halogenation and peroxidase cycle of LPO have been determined by multi-mixing stopped-flow spectroscopy. The standard reduction potentials of the redox couples compound I/native LPO, compound I/compound II of LPO, and compound II/native LPO are (1.09 +/- 0.01) V, (1.14 +/- 0.02) V, and (1.04 +/- 0.02) V, respectively, at pH 7 and 25 degrees C. Thus, for the first time, a full description of these important thermodynamic parameters of lactoperoxidase has been performed, allowing a better understanding in the substantial differences in the oxidation of two- and one-electron donors by LPO and other members of the mammalian heme peroxidase superfamily. (c) 2005 Elsevier Inc. All rights reserved.
Authors BOKU Wien:
Furtmüller Paul Georg
Jakopitsch Christa
Obinger Christian
Find related publications in this database (using NML MeSH Indexing)
Animals -
Cattle -
Lactoperoxidase - chemistry
Milk - enzymology
Oxidation-Reduction - enzymology

Find related publications in this database (Keywords)
lactoperoxidase
halogenation activity
peroxidase activity
compound I
compound II
standard reduction potential
stopped-flow spectroscopy


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