Affiliations: Institute of Medical Physics and Biophysics, Medical
Faculty, University of Leipzig, Leipzig, Germany
Note: [] Address for correspondence: Jürgen Arnhold, Institut für
Medizinische Physik und Biophysik, Universität Leipzig, Härtelstrasse
16-18, D-04107 Leipzig, Germany. Tel.: +49 341 9715705; Fax: +49 341 9715709;
E-mail: [email protected]
Abstract: The formation of chlorohydrins, bromohydrins, and iodohydrins from
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) by the
myeloperoxidase-hydrogen peroxide-halide system was evaluated by means of
matrix-assisted laser desorption/ionisation time-of-flight (MALDI-TOF) mass
spectrometry. This approach allows to detect different kinds of the
halogenation reaction even in one mass spectrum. Using a mixture of
Cl^-, Br^-, I^-, and
SCN^- at physiological concentrations, a bromination of POPC
dominates by the MPO-hydrogen peroxide-halide system. Hypothiocyanite does
apparently not react with the double bond of POPC, but increasing amounts of
SCN^- cause a decrease of the bromohydrin peaks. An
interconversion between different hypohalous acids produced by the
myeloperoxidase-hydrogen peroxide-halide system determines the pattern of
halogenohydrins in POPC. Especially, hypochlorous acid is able to oxidise
Br^- to hypobromous acid.
