These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Peroxynitrite-dependent modifications of tyrosine residues in hemoglobin. Formation of tyrosyl radical(s) and 3-nitrotyrosine.
    Author: Pietraforte D, Salzano AM, Marino G, Minetti M.
    Journal: Amino Acids; 2003 Dec; 25(3-4):341-50. PubMed ID: 14661095.
    Abstract:
    Although peroxynitrite is believed to be one of the most efficient tyrosine-nitrating species of biological relevance so far identified, its nitration efficiency is nevertheless limited. In fact, the nitrating species formed through peroxynitrite decay are caged radicals ((*)OH/(*)NO(2) or, in the presence of carbon dioxide, CO(3)(*-)/(*)NO(2)) and the fraction that escapes from the solvent cage does not exceed 30-35%. One exception may be represented by metal-containing compounds that can enhance the formation of nitrotyrosine through a bimolecular reaction with peroxynitrite. Moreover, if the metal is also regenerated in the reaction, the compound is considered a nitration catalysts and the yield of tyrosine nitration enhanced several fold. Examples of peroxynitrite-dependent nitration catalysts are the Mn-superoxide dismutase, some cytochromes and several metalloporphyrins. On the contrary, it has been claimed that some hemoproteins are scavengers of peroxynitrite and play a role in limiting its biodamaging and bioregulatory activity. In this review, we discuss the case of hemoglobin, which is probably the major target of peroxynitrite in blood. This protein has been reported to protect intracellular and extracellular targets from peroxynitrite-mediated tyrosine nitration. This property is shared with myoglobin and cytochrome c. The possible mechanisms conferring to these proteins a peroxynitrite scavenging role are discussed.
    [Abstract] [Full Text] [Related] [New Search]