Enzymatic Oxidation of Methane

• Published in: Biochemistry (Easton) Vol. 54; no. 14; pp. 2283 - 2294
• Main Authors: Sirajuddin, Sarah, Rosenzweig, Amy C
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 14-04-2015
• Subjects: Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Biocatalysis; Catalytic Domain; Methane - metabolism; Methylococcus capsulatus - enzymology; Oxidation-Reduction; Oxygenases - chemistry; Oxygenases - metabolism; Protein Conformation
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/acs.biochem.5b00198

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.