Biochemical and Biophysical Research Communications
Redox properties of the couples compound I/compound II and compound II/native enzyme of human myeloperoxidase☆
Section snippets
Materials and methods
Materials. Highly purified myeloperoxidase of a purity index (A430/A280) of at least 0.85 was obtained from Planta Naturstoffe Vertriebs GmbH (http://www.myeloperoxidase.com). Its concentration was determined using ε430=91,000 [8]. Hydrogen peroxide and nitrite solutions were prepared shortly before use. The concentration of a stock solution of H2O2 was determined using [23]. All chemicals were purchased from Sigma Chemical at the highest grade available.
Transient-state
Results and discussion
Compound II was built as described above in detail. MPO compound II is characterised by its Soret peak at 456 nm and an additional band at 630 nm. Since we followed the reaction with the diode array detector it was important to know the stability of compound II in the absence of exogenous electron donors. Upon mixing with buffer a slow transformation of compound II to the ferric enzyme is observed (rate at pH 7) as indicated by the decrease of absorbance at 456 and 630 nm and an absorbance
Acknowledgements
This work was supported by the Austrian Science Fund FWF (Grant Nos. P14187-MOB and P15660) and the German Research Foundation (Postgraduate Training Programme ‘Mechanisms and Applications of Non-Conventional Oxidation Reactions’).
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Abbreviations: MPO, myeloperoxidase; EPO, eosinophil peroxidase; LPO, lactoperoxidase; HRP, horseradish peroxidase; PorFe3+, ferric enzyme; , compound I; PorFeIV=O, compound II; Por, porphyrin ring; E′°, standard reduction potential; K′ equilibrium constant at pH 7.