颗粒性甲烷单加氧酶的金属重构及pmoB亚基的异源表达
Metal reconstitution of particulate methane monooxygenase and heterologous expression of the pmoB subunit.
作者信息
Smith Stephen M, Balasubramanian Ramakrishnan, Rosenzweig Amy C
机构信息
Department of Molecular Biosciences, Northwestern University, Evanston, Illinois, USA.
出版信息
Methods Enzymol. 2011;495:195-210. doi: 10.1016/B978-0-12-386905-0.00013-9.
Abstract
Particulate methane monooxygenase (pMMO) is a multisubunit metalloenzyme complex used by methanotrophic bacteria to oxidize methane in the first step of carbon assimilation and energy production. In this chapter, we detail methods to prepare metal free (apo) membrane-bound pMMO and to reconstitute apo pMMO with metal ions. We also describe protocols to clone, express, and refold metal-loaded soluble domain constructs of the pmoB subunit. These approaches were used to address fundamental questions concerning the metal content and location of the pMMO active site.
摘要
颗粒性甲烷单加氧酶（pMMO）是一种多亚基金属酶复合物，甲烷营养细菌利用它在碳同化和能量产生的第一步中氧化甲烷。在本章中，我们详细介绍了制备无金属（脱辅基）膜结合pMMO以及用金属离子重构脱辅基pMMO的方法。我们还描述了克隆、表达和重折叠pmoB亚基的金属负载可溶性结构域构建体的方案。这些方法被用于解决有关pMMO活性位点的金属含量和位置的基本问题。
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