Mechanistic study of singlet oxygen formation by tryptophan and tyrosine peroxides...
| Full text | |
| Author(s): |
Marques, Emerson Finco
;
Medeiros, Marisa H. G.
;
Di Mascio, Paolo
[1]
Total Authors: 3
|
| Affiliation: | [1] Univ Sao Paulo, Dept Bioquim, Inst Quim, BR-05508000 Sao Paulo, SP - Brazil
Total Affiliations: 1
|
| Document type: | Journal article |
| Source: | Journal of Mass Spectrometry; v. 52, n. 11, p. 739-751, NOV 2017. |
| Web of Science Citations: | 3 |
| Abstract | |
Singlet molecular oxygen (O-1(2)) is generated in biological systems and reacts with different biomolecules. Proteins are a major target for O-1(2), and His, Tyr, Met, Cys, and Trp are oxidized at physiological pH. In the present study, the modification of lysozyme protein by O-1(2) was investigated using mass spectrometry approaches. The experimental findings showed methionine, histidine, and tryptophan oxidation. The experiments were achieved using {[}O-18]-labeled O-1(2) 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 {[}O-18]-labeling atoms in different amino acids. (AU) | |
| FAPESP's process: | 12/12663-1 - Singlet molecular oxygen and peroxides in chemical biology |
| Grantee: | Paolo Di Mascio |
| Support type: | Research Projects - Thematic Grants |
| FAPESP's process: | 13/07937-8 - Redoxome - Redox Processes in Biomedicine |
| Grantee: | Ohara Augusto |
| Support type: | Research Grants - Research, Innovation and Dissemination Centers - RIDC |