The Cu^ICu^ICu^I tricopper cluster complex is the only known catalyst capable of efficient methane oxidation near room temperature similar to the particulate methane monooxygenase (pMMO). Here, we compare the turnover of the Cu^ICu^ICu^I tricopper catalyst with the biochemistry of the functional pMMO. Insights into the turnover of the biomimetic tricopper catalyst are derived from anaerobic electrospray mass spectrometry (ESI‐MS) and high‐resolution ESI‐MS (HR‐ESI‐MS). We follow activation of the tricopper cluster with O₂/H₂O₂ by rapid‐freeze‐quench ESI‐MS, high‐resolution cold‐spray ionization mass spectrometry (HR‐CSI‐MS) and electron paramagnetic resonance spectroscopy, capturing all the species participating in the activation and deactivation pathways of the turnover cycle. The reactivity of the activated tricopper complex toward alkane oxidation is essentially the same as the biochemistry reported earlier for pMMO from Methylococcus capsulatus (Bath).

中文翻译：

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甲烷氧化Tricopper簇催化剂的营业额：对颗粒甲烷单加氧酶（pMMO）的机制的影响。

与颗粒甲烷单加氧酶（pMMO）相似，Cu ^I Cu ^I Cu ^I三铜簇簇配合物是唯一已知的能够在室温附近有效甲烷氧化的催化剂。在这里，我们将Cu ^I Cu ^I Cu ^I三铜催化剂的转化率与功能性pMMO的生物化学进行了比较。仿生三铜催化剂转化率的见解来自厌氧电喷雾质谱（ESI-MS）和高分辨率ESI-MS（HR-ESI-MS）。我们用O ₂ / H ₂ O ₂激活三铜簇通过快速冷冻猝灭ESI-MS，高分辨率冷喷雾电离质谱（HR-CSI-MS）和电子顺磁共振波谱法，捕获了参与周转周期激活和失活途径的所有物种。的活化tricopper朝向烷烃氧化复合物中的反应性是基本相同的生物化学为单加氧酶来自先前报道甲基球菌荚膜（浴）。