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首页> 外文期刊>Journal of the Korean Society for Applied Biological Chemistry >Peroxidase Inactivation by Covalent Modification with Phenoxyl Radical during Phenol Oxidation
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Peroxidase Inactivation by Covalent Modification with Phenoxyl Radical during Phenol Oxidation

机译：在苯酚氧化过程中通过与苯氧基自由基共价修饰使过氧化物酶失活

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摘要

The mechanism-based inactivation of peroxidases limits the usefulness of these versatile enzymes. In this study, we propose a dominant inactivation mechanism for peroxidase during phenol oxidation. Two peroxidases, Coprinus cinereus peroxidase (CiP) and horseradish peroxidase isozyme C (HRPC) showed much higher inactivation rates after simultaneous addition of phenol and hydrogen peroxide, whereas addition of hydrogen peroxide alone or polymeric products had relatively little impact on peroxidase activity. During the oxidation of a phenol substrate, the molecular weights of polypeptides originating from inactivated peroxidases were slightly increased, and a large fraction of CiP and HRPC hemes remained intact even after phenoxyl radical coupling. Our study strongly supports the hypothesis that the inactivation of a peroxidase during the oxidation of phenolic compounds occurs by a covalent modification of the peroxidase polypeptide chain with a phenoxyl radical. These findings will elucidate the method of inactivation for peroxidase and other heme proteins.
机译：过氧化物酶的基于机制的失活限制了这些通用酶的实用性。在这项研究中，我们提出了酚氧化过程中过氧化物酶的主要失活机制。在同时添加苯酚和过氧化氢后，两种鬼臼鬼臼过氧化物酶（CiP）和辣根过氧化物酶同工酶C（HRPC）表现出更高的失活率，而单独添加过氧化氢或聚合产物对过氧化物酶活性的影响相对较小。在酚底物的氧化过程中，源自灭活的过氧化物酶的多肽的分子量略有增加，即使在苯氧基自由基偶联后，大部分的CiP和HRPC血红素仍保持完整。我们的研究强烈支持以下假设：酚类化合物氧化过程中过氧化物酶的失活是通过过氧化物酶多肽链与苯氧基自由基的共价修饰而发生的。这些发现将阐明过氧化物酶和其他血红素蛋白失活的方法。

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