Biochemistry of aerobic biological methane oxidation

Koo, Christopher W.; Rosenzweig, Amy C.

doi:10.1039/d0cs01291b

Biochemistry of aerobic biological methane oxidation

Journal Article · Sun Jan 24 23:00:00 EST 2021 · Chemical Society Reviews

DOI:https://doi.org/10.1039/d0cs01291b· OSTI ID:1852178

^[1]; ^[2]

Northwestern Univ., Evanston, IL (United States); OSTI
Northwestern Univ., Evanston, IL (United States)

Methanotrophic bacteria represent a potential route to methane utilization and mitigation of methane emissions. In the first step of their metabolic pathway, aerobic methanotrophs use methane monooxygenases (MMOs) to activate methane, oxidizing it to methanol. There are two types of MMOs: a particulate, membrane-bound enzyme (pMMO) and a soluble, cytoplasmic enzyme (sMMO). The two MMOs are completely unrelated, with different architectures, metal cofactors, and mechanisms. The more prevalent of the two, pMMO, is copper-dependent, but the identity of its copper active site remains unclear. By contrast, sMMO uses a diiron active site, the catalytic cycle of which is well understood. Here we review the current state of knowledge for both MMOs, with an emphasis on recent developments and emerging hypotheses. In addition, we discuss obstacles to developing expression systems, which are needed to address outstanding questions and to facilitate future protein engineering efforts.

View Accepted Manuscript (DOE)

Research Organization:: Northwestern Univ., Evanston, IL (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: SC0016284

OSTI ID:: 1852178

Alternate ID(s):: OSTI ID: 1762517

Journal Information:: Chemical Society Reviews, Journal Name: Chemical Society Reviews Journal Issue: 5 Vol. 50; ISSN 0306-0012

Publisher:: Royal Society of ChemistryCopyright Statement

Country of Publication:: United States

Language:: English

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