A comparative study of ribonuclease and lysozyme oxidation and nitration by peroxynitrite and myeloperoxidase
Vaz, SM; Prado, FA; Di Mascio, P; Augusto, O
HERO ID
975856
Reference Type
Journal Article
Subtype
Abstract
Year
2008
Language
English
| HERO ID | 975856 |
|---|---|
| Material Type | Abstract |
| In Press | No |
| Year | 2008 |
| Title | A comparative study of ribonuclease and lysozyme oxidation and nitration by peroxynitrite and myeloperoxidase |
| Authors | Vaz, SM; Prado, FA; Di Mascio, P; Augusto, O |
| Journal | Free Radical Biology and Medicine |
| Volume | 45 |
| Issue | Suppl. |
| Page Numbers | S75-S75 |
| Abstract | Protein oxidation and nitration are commonly employed as biomarkers of the formation of oxidative and nitro-oxidative species in cells, experimental animals and human tissues. However, there is a lack of information on the behavior of important nitro-oxidative mediators, such as peroxynitrite and myeloperoxidase towards protein targets. Here we compared the oxidative modifications promoted by 1 mM peroxynitrite and MPO/H2O2 (1 mM)/NO2 − (1 mM) on ribonuclease (6Tyr) and lysozyme (3Tyr/6Trp) at pHs 5.4, 6.4, and 7.4. EPR and product analysis (HPLC/MS-ESI of pronase hydrolysates and HPLC-MSMaldi-ToF and MS-ESI of tryptic digests) provided the following results. (I) Total ribonuclease and lysozyme oxidation, including protein radical formation, was higher at pH 5.4 and 7.4 for MPO and peroxynitrite, respectively. (II) in the Trp-containing lysozyme the main target was Trp62/63 and Tyr23 for peroxynitrite and MPO, respectively. (III) in ribonuclease, peroxynitrite modified mainly accessible Tyr115 and Tyr92/97 whereas, MPO modified most Tyr residues suggesting protein unfolding. (IV) Both oxidants produced hydroxylated products of Trp (lysozyme-Trp62) and Tyr (ribonuclease-Tyr73) in surface-exposed residues. in conclusion, the results indicate that Trp residues are particularly important target for peroxynitrite. Also, that MPO is likely to be a more efficient promoter of protein nitro-oxidative damage at acid pH. Supported by FAPESP and CNPq. |
| Wosid | WOS:000260867900212 |
| Url | http://www.sciencedirect.com/science/article/pii/S0891584908006242 |
| Is Certified Translation | No |
| Dupe Override | No |
| Conference Location | Indianapolis, IN |
| Conference Name | Society for Free Radical Biology and Medicine15th Annual Meeting |
| Conference Date | November 19-23, 2008 |
| Is Public | Yes |
| Language Text | English |
| Relationship(s) |
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