title: Biocatalysts for methane conversion: big progress on breaking a small substrate.
abstract: Nature utilizes two groups of enzymes to catalyze methane conversions, methyl-coenzyme M reductases (MCRs) and methane monooxygenases (MMOs). These enzymes have been difficult to incorporate into industrial processes due to their complexity, poor stability, and lack of recombinant tractability. Despite these issues, new ways of preparing and stabilizing these enzymes have recently been discovered, and new mechanistic insight into how MCRs and MMOs break the C-H bond in nature's most inert hydrocarbon have been obtained. This review focuses on recent findings in the methane biocatalysis field, and discusses the impact of these finding on designing MMO and MCR-based biotechnologies.
authors: Departments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, IL 60208, USA.
authors: Thomas J
authors: TJ
authors: Lawton
authors: Departments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, IL 60208, USA. Electronic address: amyr@northwestern.edu.
authors: Amy C
authors: AC
authors: Rosenzweig
mesh_terms: D055162:Biocatalysis; D008697:Methane / Q000378:metabolism*; D010088:Oxidoreductases / Q000378:metabolism; D010105:Oxygenases / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D011994:Recombinant Proteins; D010088:Oxidoreductases; D010105:Oxygenases; C021555:methane monooxygenase; C021572:methyl coenzyme M reductase; D008697:Methane