Hydrogen peroxide as an effecter on the inactivation of particulate methane monooxygenase under aerobic conditions
Hydrogen peroxide as an effecter on the inactivation of particulate methane monooxygenase under aerobic conditions
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DOI：
10.1016/j.molcatb.2008.09.005
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发表时间：
2009-05-01
影响因子：
--
通讯作者：
Okura, Ichiro
中科院分区：
文献类型：
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作者：
Miyaji, Akimitsu;Suzuki, Masashi;Okura, Ichiro
颗粒甲烷单加氧酶（pMMO）是一种含铜的膜蛋白，在有氧条件下催化甲烷羟基化。我们发现，过氧化氢酶的活性增加，这意味着过氧化氢（H2O2）产生的pMMO与duroquinol，pMMO的电子供体，和所产生的H2O2抑制pMMO活性。此外，可逆抑制pMMO与H2O2的观察后，处理pMMO与H2O2，然后通过添加过氧化氢酶，和H2O2的形成与duroquinol的pMMO检测使用荧光探针。通过电子顺磁共振测量的pMMO中的2型铜的氧化还原行为表明，H2O2再氧化的2型铜在pMMO中还原杜醌醇。(C)2008 Elsevier B.V.保留所有权利。
Particulate methane monooxygenase (pMMO), a copper-containing membrane protein, catalyzes methane hydroxylation under aerobic conditions. We found that the activity of pMMO was increased by catalase, implying that hydrogen peroxide (H2O2) is generated by pMMO with duroquinol, an electron donor for pMMO, and that the generated H2O2 inhibits pMMO activity. In addition, reversible inhibition of pMMO with H2O2 was observed upon treatment of pMMO with H2O2 followed by the addition of catalase, and H2O2 formation by pMMO with duroquinol was detected using a fluorescence probe. The redox behavior of type 2 copper in pMMO measured by the electron paramagnetic resonance revealed that H2O2 re-oxidizes the type 2 copper in pMMO reduced with duroquinol. (C) 2008 Elsevier B.V. All rights reserved.