From micelles to bicelles: Effect of the membrane on particulate methane monooxygenase activity

Ro, Soo Y.; Ross, Matthew O.; Deng, Yue Wen; Batelu, Sharon; Lawton, Thomas J.; Hurley, Joseph D.; Stemmler, Timothy L.; Hoffman, Brian M.; Rosenzweig, Amy C.

doi:10.1074/jbc.RA118.003348

Title: From micelles to bicelles: Effect of the membrane on particulate methane monooxygenase activity

Journal Article · 08 May 2018 · Journal of Biological Chemistry

DOI: https://doi.org/10.1074/jbc.RA118.003348 · OSTI ID:1544885

Ro, Soo Y. ^[1]; Ross, Matthew O. ^[1]; Deng, Yue Wen ^[1]; Batelu, Sharon ^[2]; Lawton, Thomas J. ^[1]; Hurley, Joseph D. ^[1]; Stemmler, Timothy L. ^[2]; Hoffman, Brian M. ^[1];

^[1]

Northwestern Univ., Evanston, IL (United States)
Wayne State Univ., Detroit, MI (United States)

Particulate methane monooxygenase (pMMO) is a copper-dependent integral membrane metalloenzyme that converts methane to methanol in methanotrophic bacteria. Studies of isolated pMMO have been hindered by loss of enzymatic activity upon its removal from the native membrane. To characterize pMMO in a membrane-like environment, we reconstituted pMMOs from Methylococcus (Mcc.) capsulatus (Bath) and Methylomicrobium (Mm.) alcaliphilum 20Z into bicelles. Reconstitution into bicelles recovers methane oxidation activity lost upon detergent solubilization and purification without substantial alterations to copper content or copper electronic structure, as observed by electron paramagnetic resonance (EPR) spectroscopy. These findings suggest that loss of pMMO activity upon isolation is due to removal from the membranes rather than caused by loss of the catalytic copper ions. A 2.7 Å resolution crystal structure of pMMO from Mm. alcaliphilum 20Z reveals a mononuclear copper center in the PmoB subunit and indicates that the transmembrane PmoC subunit may be conformationally flexible. Finally, results from extended X-ray absorption fine structure (EXAFS) analysis of pMMO from Mm. alcaliphilum 20Z were consistent with the observed monocopper center in the PmoB subunit. These results underscore the importance of studying membrane proteins in a membrane-like environment and provide valuable insight into pMMO function.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: National Institutes of Health (NIH)

Grant/Contract Number:: AC02-76SF00515

OSTI ID:: 1544885

Journal Information:: Journal of Biological Chemistry, Vol. 293, Issue 27; ISSN 0021-9258

Publisher:: American Society for Biochemistry and Molecular BiologyCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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59 BASIC BIOLOGICAL SCIENCES
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
copper monooxygenase
metalloenzyme
crystal structure
biofuel
biotechnology
protein-lipid interaction
membrane protein
bicelle
copper metalloenzyme
methane oxidation
methanotroph
particulate methane monooxygenase

Title: From micelles to bicelles: Effect of the membrane on particulate methane monooxygenase activity

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