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可溶性甲烷单加氧酶。

Soluble Methane Monooxygenase.

机构信息

Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA; email:

出版信息

Annu Rev Biochem. 2019 Jun 20;88:409-431. doi: 10.1146/annurev-biochem-013118-111529. Epub 2019 Jan 11.

Abstract

Aerobic life is possible because the molecular structure of oxygen (O) makes direct reaction with most organic materials at ambient temperatures an exceptionally slow process. Of course, these reactions are inherently very favorable, and they occur rapidly with the release of a great deal of energy at high temperature. Nature has been able to tap this sequestered reservoir of energy with great spatial and temporal selectivity at ambient temperatures through the evolution of oxidase and oxygenase enzymes. One mechanism used by these enzymes for O activation has been studied in detail for the soluble form of the enzyme methane monooxygenase. These studies have revealed the step-by-step process of O activation and insertion into the ultimately stable C-H bond of methane. Additionally, an elegant regulatory mechanism has been defined that enlists size selection and quantum tunneling to allow methane oxidation to occur specifically in the presence of more easily oxidized substrates.

摘要

有氧生活之所以成为可能,是因为氧(O)的分子结构使得其在环境温度下与大多数有机物质直接反应成为一个异常缓慢的过程。当然,这些反应在本质上是非常有利的,并且它们在高温下会迅速发生,同时释放大量能量。通过氧化酶和加氧酶的进化,自然界已经能够在环境温度下以极大的空间和时间选择性利用这种被隔离的能量库。这些酶用于 O 激活的一种机制已经在可溶性甲烷单加氧酶的形式下被详细研究。这些研究揭示了 O 激活和插入甲烷最终稳定的 C-H 键的逐步过程。此外,已经定义了一种优雅的调节机制,该机制利用尺寸选择和量子隧穿来允许甲烷氧化仅在更容易氧化的底物存在下发生。

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