Format

Send to

Choose Destination
Biochemistry. 2015 Apr 14;54(14):2283-94. doi: 10.1021/acs.biochem.5b00198. Epub 2015 Apr 1.

Enzymatic oxidation of methane.

Author information

1
Departments of Molecular Biosciences and of Chemistry, Northwestern University, Evanston, Illinois 60208, United States.

Abstract

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.

PMID:
25806595
PMCID:
PMC5257249
DOI:
10.1021/acs.biochem.5b00198
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for American Chemical Society Icon for PubMed Central
Loading ...
Support Center