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本文引用的文献

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Hydrolytic catalysis and structural stabilization in a designed metalloprotein.设计金属蛋白中的水解催化和结构稳定
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Homogeneous catalytic O2 reduction to water by a cytochrome c oxidase model with trapping of intermediates and mechanistic insights.细胞色素 c 氧化酶模型对氧的均相催化还原为水，同时中间体被捕获并对反应机理有深入了解。
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The cytochrome bd respiratory oxygen reductases.细胞色素bd呼吸氧还原酶
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Proton-coupled electron transfer in cytochrome oxidase.细胞色素氧化酶中的质子耦合电子转移
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Rational design of a structural and functional nitric oxide reductase.结构与功能一氧化氮还原酶的合理设计。
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Exploitation of binding energy for catalysis and design.利用结合能进行催化与设计。
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The cytochrome ba3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping.嗜热栖热菌的细胞色素ba3氧还原酶利用单一输入通道将质子传递至活性位点并用于质子泵浦。
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一种设计的功能金属酶，可将 O2 转化为 H2O，超过一千次循环。

A designed functional metalloenzyme that reduces O2 to H2O with over one thousand turnovers.

机构信息

Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.

出版信息

Angew Chem Int Ed Engl. 2012 Jun 4;51(23):5589-92. doi: 10.1002/anie.201201981. Epub 2012 Apr 26.

DOI:10.1002/anie.201201981
PMID:22539151
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3461324/
Abstract

[Image: see text] Rational design of functional enzymes with high turnovers is a significant challenge, especially those with complex active site and difficult reactions, such as in respiratory oxidases. Introducing 2 His and 1 Tyr into myoglobin resulted in designed enzymes that reduce O to HO with > 1000 turnovers and minimal release of reactive oxygen species. This also showed that presence and positioning of Tyr, not Cu, are critical for activity.

摘要

[图片：见正文]具有高周转率的功能酶的合理设计是一项重大挑战，特别是那些具有复杂活性位点和困难反应的酶，如呼吸氧化酶。将 2 个组氨酸和 1 个酪氨酸引入肌红蛋白中，得到了设计酶，这些酶可将 O 还原为 HO，周转率超过 1000 次，且活性氧的释放最小。这也表明，酪氨酸的存在和定位（而非 Cu）对活性至关重要。