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The cryoEM structures of the MMOH-MMOR complex


EMSL Project ID
51325

Abstract

Methane to methanol conversion is critical for environmental health, reducing greenhouse gas, and utilizing the natural gas as an alternative energy source. Methanotrophic bacteria utilize the methane (CH4) as a sole source of carbon and energy by oxidizing and breaking the highly stable C-H bond. This can be achieved via the enzyme complex called methane monooxygenase (MMO). Soluble methane monooxygenase (sMMO) is a multi-component protein complex comprising a 245-kDa (alpha beta gamma)2 hydroxylase MMOH, a 16-kDa regulatory protein MMOB, a 38-kDa electron-transfer reductase MMOR, and 12-kDa potential MMO inhibitory subunit (MMOD). Since the maximum catalytic activity of sMMO is only achieved via the interplay of MMOH with three auxiliary subunits, structural elucidation is a key to understand its chemistry and to develop bio-mimetic catalysts. In this project, we would like to illustrate how auxiliary subunits interact with MMOH using single-particle cryo-EM.

Project Details

Start Date
2020-05-15
End Date
2021-03-17
Status
Closed

Team

Principal Investigator

Uhn-soo Cho
Institution
University of Michigan

Team Members

Byung Chul Kim
Institution
University of Michigan

Nancy Meyer
Institution
Oregon Health & Science University