Enzymatic oxidation of methane.
Enzymatic oxidation of methane.
复制标题
甲烷的酶促氧化。
DOI：
10.1021/acs.biochem.5b00198
复制
发表时间：
2015-04-14
期刊：
影响因子：
2.9
通讯作者：
Rosenzweig AC
中科院分区：
文献类型：
--
作者：
Sirajuddin S;Rosenzweig AC
甲烷单加氧酶（MMO）是在甲烷氧化细菌中催化甲烷氧化为甲醇的酶。甲烷多金属氧化物作为新型甲烷生物转化工艺的潜在目标，近年来引起了人们的广泛关注。有两种不同类型的MMO，可溶性细胞质MMO（sMMO）和膜结合颗粒状MMO（pMMO）。两者都在复杂的多亚基支架内的金属中心氧化甲烷，但结构、活性位点和化学机制完全不同。这篇当前主题的综述文章侧重于两种MMO的整体架构、活性位点结构、底物反应性、蛋白质-蛋白质相互作用和化学机制，重点是基本方面。此外，最近的进展，包括新的细节之间的相互作用的sMMO组件，sMMO中间体的表征，并朝着理解的pMMO金属中心的进展突出。这里总结的工作为那些有兴趣利用MMO进行生物技术应用的人提供了指导。
Methane monooxygenases (MMOs) are enzymes that catalyze the oxidation of methane to methanol in methanotrophic bacteria. As potential targets for new gas-to-liquid methane bioconversion processes, MMOs have attracted intense attention in recent years. There are two distinct types of MMO, a soluble, cytoplasmic MMO (sMMO) and a membrane-bound, particulate MMO (pMMO). Both oxidize methane at metal centers within a complex, multisubunit scaffold, but the structures, active sites, and chemical mechanisms are completely different. This Current Topic review article focuses on the overall architectures, active site structures, substrate reactivities, protein–protein interactions, and chemical mechanisms of both MMOs, with an emphasis on fundamental aspects. In addition, recent advances, including new details of interactions between the sMMO components, characterization of sMMO intermediates, and progress toward understanding the pMMO metal centers are highlighted. The work summarized here provides a guide for those interested in exploiting MMOs for biotechnological applications.