Lysozyme oxidation by singlet molecular oxygen: Peptide characterization using [18 O]-labeling oxygen and nLC-MS/MS.
Emerson Finco MarquesMarisa H G MedeirosPaolo Di MascioPublished in: Journal of mass spectrometry : JMS (2018)
Singlet molecular oxygen (1 O2 ) is generated in biological systems and reacts with different biomolecules. Proteins are a major target for 1 O2 , and His, Tyr, Met, Cys, and Trp are oxidized at physiological pH. In the present study, the modification of lysozyme protein by 1 O2 was investigated using mass spectrometry approaches. The experimental findings showed methionine, histidine, and tryptophan oxidation. The experiments were achieved using [18 O]-labeled 1 O2 released from thermolabile endoperoxides in association with nano-scale liquid chromatography coupled to electrospray ionization mass spectrometry. The structural characterization by nLC-MS/MS of the amino acids in the tryptic peptides of the proteins showed addition of [18 O]-labeling atoms in different amino acids.
Keyphrases
- liquid chromatography tandem mass spectrometry
- amino acid
- liquid chromatography
- mass spectrometry
- simultaneous determination
- ms ms
- tandem mass spectrometry
- high performance liquid chromatography
- high resolution mass spectrometry
- ultra high performance liquid chromatography
- gas chromatography
- hydrogen peroxide
- capillary electrophoresis
- high resolution
- tyrosine kinase
- single molecule
- visible light
- quantum dots
- low density lipoprotein
- pet imaging
- nitric oxide
- binding protein