Catalytic machinery of methane oxidation in particulate methane monooxygenase (pMMO)

2021 ◽  
Vol 225 ◽  
pp. 111602
Author(s):  
Sunney I. Chan ◽  
Wei-Hau Chang ◽  
Shih-Hsin Huang ◽  
Hsin-Hung Lin ◽  
Steve S.-F. Yu
ChemCatChem ◽  
2020 ◽  
Vol 12 (11) ◽  
pp. 3088-3096
Author(s):  
Yu‐Hsuan Chen ◽  
Chang‐Quan Wu ◽  
Pei‐Hua Sung ◽  
Sunney I. Chan ◽  
Peter Ping‐Yu Chen

Science ◽  
2019 ◽  
Vol 364 (6440) ◽  
pp. 566-570 ◽  
Author(s):  
Matthew O. Ross ◽  
Fraser MacMillan ◽  
Jingzhou Wang ◽  
Alex Nisthal ◽  
Thomas J. Lawton ◽  
...  

Bacteria that oxidize methane to methanol are central to mitigating emissions of methane, a potent greenhouse gas. The nature of the copper active site in the primary metabolic enzyme of these bacteria, particulate methane monooxygenase (pMMO), has been controversial owing to seemingly contradictory biochemical, spectroscopic, and crystallographic results. We present biochemical and electron paramagnetic resonance spectroscopic characterization most consistent with two monocopper sites within pMMO: one in the soluble PmoB subunit at the previously assigned active site (CuB) and one ~2 nanometers away in the membrane-bound PmoC subunit (CuC). On the basis of these results, we propose that a monocopper site is able to catalyze methane oxidation in pMMO.


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