Structure and activity of particulate methane monooxygenase arrays in methanotrophs

Yanan Zhu, Christopher W. Koo, C. Keith Cassidy, Matthew C. Spink, Tao Ni, Laura C. Zanetti-Domingues, Benji Bateman, Marisa L. Martin-Fernandez, Juan Shen, Yuewen Sheng, Yun Song, Zhengyi Yang, Amy C. Rosenzweig () and Peijun Zhang ()
Additional contact information
Yanan Zhu: University of Oxford
Christopher W. Koo: Northwestern University
C. Keith Cassidy: University of Oxford
Matthew C. Spink: Diamond Light Source, Harwell Science and Innovation Campus
Tao Ni: University of Oxford
Laura C. Zanetti-Domingues: Rutherford Appleton Laboratory
Benji Bateman: Rutherford Appleton Laboratory
Marisa L. Martin-Fernandez: Rutherford Appleton Laboratory
Juan Shen: University of Oxford
Yuewen Sheng: Diamond Light Source, Harwell Science and Innovation Campus
Yun Song: Diamond Light Source, Harwell Science and Innovation Campus
Zhengyi Yang: Diamond Light Source, Harwell Science and Innovation Campus
Amy C. Rosenzweig: Northwestern University
Peijun Zhang: University of Oxford

Nature Communications, 2022, vol. 13, issue 1, 1-10

Abstract: Abstract Methane-oxidizing bacteria play a central role in greenhouse gas mitigation and have potential applications in biomanufacturing. Their primary metabolic enzyme, particulate methane monooxygenase (pMMO), is housed in copper-induced intracytoplasmic membranes (ICMs), of which the function and biogenesis are not known. We show by serial cryo-focused ion beam (cryoFIB) milling/scanning electron microscope (SEM) volume imaging and lamellae-based cellular cryo-electron tomography (cryoET) that these ICMs are derived from the inner cell membrane. The pMMO trimer, resolved by cryoET and subtomogram averaging to 4.8 Å in the ICM, forms higher-order hexagonal arrays in intact cells. Array formation correlates with increased enzymatic activity, highlighting the importance of studying the enzyme in its native environment. These findings also demonstrate the power of cryoET to structurally characterize native membrane enzymes in the cellular context.

Date: 2022
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DOI: 10.1038/s41467-022-32752-9

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