| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 7560729 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2015 | 29 Pages |
Abstract
High-resolution mass spectrometry has been used to study the inactivation of the particulate methane monooxygenase (pMMO) in Methylococcus capsulatus (Bath) by acetylene. The results show that this inhibitor is oxidized to ketene at the catalytic site of the enzyme, which subsequently acetylates K196 of the PmoC subunit in the membrane.128
Keywords
pMMOMethylococcus capsulatus (Bath)DHBMMODDMMECNBN-PAGETOF-MSLC–MS/MSAmmonia monooxygenaseAcetonitrileAcetyleneFormic acidblue native-polyacrylamide gel electrophoresisSDS-PAGESodium dodecyl sulfate polyacrylamide gel electrophoresisEPRElectron paramagnetic resonancedihydroxybenzoic acidComputational simulationMass spectrometryTime-of-flight mass spectrometryAMOMechanism-based inactivationreduced form of nicotinamide adenine dinucleotidematrix assisted laser desorption ionizationMASCOTMALDImethane monooxygenaseParticulate methane monooxygenaseNADHliquid chromatographyliquid chromatography–tandem mass spectrometryGas chromatography
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Minh D. Pham, Ya-Ping Lin, Quan Van Vuong, Penumaka Nagababu, Brian T.-A. Chang, Kok Yaoh Ng, Chein-Hung Chen, Chau-Chung Han, Chung-Hsuan Chen, Mai Suan Li, Steve S.-F. Yu, Sunney I. Chan,