髓过氧化物酶氧化态参与硫醇的髓过氧化物酶 - 氧化酶氧化反应。
Myeloperoxidase oxidation states involved in myeloperoxidase-oxidase oxidation of thiols.
作者信息
Svensson B E
机构信息
Research and Development Laboratories, Astra Alab AB, Södertälje, Sweden.
出版信息
Biochem J. 1988 Dec 15;256(3):751-5. doi: 10.1042/bj2560751.
The changes in the oxidation state of the leucocyte enzyme myeloperoxidase, induced by buffer and thiols, were studied with visible-light-absorption spectroscopy. It was concluded that phosphate buffer contains small amounts of H2O2 and that thiols, when added to buffer, induce the generation of minute amounts of superoxide radical anion. These minute amounts of reduced oxygen species are suggested to account for the initiation of myeloperoxidase-oxidase oxidation of thiols. Myeloperoxidase was found to be in its Compound III oxidation state during myeloperoxidase-oxidase oxidation of thiols. However, myeloperoxidase-mediated oxidation of thiols with concomitant O2 consumption can also occur with myeloperoxidase in its Compound II oxidation state. These studies indicate that the ferro and Compound III oxidation states may not be essential intermediates in myeloperoxidase-oxidase oxidation of thiols, but rather that the formation of the Compound III oxidation state retards the reaction.
利用可见光吸收光谱法研究了缓冲液和硫醇诱导的白细胞酶髓过氧化物酶氧化态的变化。得出的结论是，磷酸盐缓冲液含有少量的过氧化氢，并且当向缓冲液中添加硫醇时，会诱导产生微量的超氧阴离子自由基。这些微量的活性氧被认为是硫醇的髓过氧化物酶 - 氧化酶氧化起始的原因。在硫醇的髓过氧化物酶 - 氧化酶氧化过程中，发现髓过氧化物酶处于其化合物III氧化态。然而，髓过氧化物酶介导的硫醇氧化并伴随氧气消耗，也可以在髓过氧化物酶处于化合物II氧化态时发生。这些研究表明，亚铁和化合物III氧化态可能不是硫醇的髓过氧化物酶 - 氧化酶氧化中的必需中间体，而是化合物III氧化态的形成会阻碍反应。
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