Arnhold Jürgen, Furtmüller Paul G, Obinger Christian
Institute of Medical Physics and Biophysics, School of Medicine, University of Leipzig, Leipzig, Germany.
Redox Rep. 2003;8(4):179-86. doi: 10.1179/135100003225002664.
The heme-containing enzyme myeloperoxidase (MPO) is secreted from polymorphonuclear leukocytes and monocytes. It is involved in host defence and inflammation by oxidation of numerous small molecules. This review summarises our current results on the determination of redox properties of all intermediates involved in the halogenation and peroxidase cycle of MPO. The standard reduction potentials of the redox couples compound I/native MPO, compound I/compound II of MPO, and compound II/native MPO have been determined to be 1.16 V, 1.35 V, and 0.97 V, respectively, at pH 7 and 25 degrees C. Thus, for the first time, a full description of these important thermodynamic parameters of myeloperoxidase has been performed, allowing a better understanding of its extraordinary reactivity.
含血红素的髓过氧化物酶（MPO）由多形核白细胞和单核细胞分泌。它通过氧化多种小分子参与宿主防御和炎症反应。本综述总结了我们目前关于MPO卤化和过氧化物酶循环中所有中间体氧化还原性质测定的结果。在pH 7和25摄氏度下，氧化还原对化合物I/天然MPO、MPO的化合物I/化合物II以及化合物II/天然MPO的标准还原电位分别测定为1.16 V、1.35 V和0.97 V。因此，首次对髓过氧化物酶这些重要的热力学参数进行了全面描述，有助于更好地理解其非凡的反应活性。
