4.5 Review Book Chapter

3-Nitrotyrosine and related derivatives in proteins: precursors, radical intermediates and impact in function

Journal

PROTEIN OXIDATION
Volume 64, Issue 1, Pages 111-133

Publisher

PORTLAND PRESS LTD
DOI: 10.1042/EBC20190052

Keywords

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Funding

  1. Comision Sectorial de Investigacion Cientifica (CSIC), Universidad de la Republica, Uruguay
  2. Comision Academica de Posgrado (CAP), Universidad de la Republica, Uruguay
  3. PEDECIBA, Universidad de la Republica, Uruguay
  4. Espacio Interdisciplinario, Universidad de la Republica, Uruguay
  5. Universidad de Buenos Aires, Argentina
  6. CONICET, Argentina

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Oxidative post-translational modification of proteins by molecular oxygen (O-2)- and nitric oxide ((NO)-N-center dot)-derived reactive species is a usual process that occurs in mammalian tissues under both physiological and pathological conditions and can exert either regulatory or cytotoxic effects. Although the side chain of several amino acids is prone to experience oxidative modifications, tyrosine residues are one of the preferred targets of one-electron oxidants, given the ability of their phenolic side chain to undergo reversible one-electron oxidation to the relatively stable tyrosyl radical. Naturally occurring as reversible catalytic intermediates at the active site of a variety of enzymes, tyrosyl radicals can also lead to the formation of several stable oxidative products through radical-radical reactions, as is the case of 3-nitrotyrosine (NO(2)Tyr). The formation of NO(2)Tyr mainly occurs through the fast reaction between the tyrosyl radical and nitrogen dioxide ((NO2)-N-center dot). One of the key endogenous nitrating agents is peroxynitrite (ONOO-), the product of the reaction of superoxide radical (O-2(center dot-)) with (NO)-N-center dot, but ONOO--independent mechanisms of nitration have been also disclosed. This chemical modification notably affects the physicochemical properties of tyrosine residues and because of this, it can have a remarkable impact on protein structure and function, both in vitro and in vivo. Although low amounts of NO(2)Tyr are detected under basal conditions, significantly increased levels are found at pathological states related with an overproduction of reactive species, such as cardiovascular and neurodegenerative diseases, inflammation and aging. While NO(2)Tyr is a well-established stable oxidative stress biomarker and a good predictor of disease progression, its role as a pathogenic mediator has been laboriously defined for just a small number of nitrated proteins and awaits further studies.

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