Reactivity of hydroxyl with tyrosine in aqueous solution studied by pulse radiolysis

Solar, Sonja; Solar, W.; Getoff, N.

doi:10.1021/j150654a030

Cited by 94 publications

(70 citation statements)

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“…Tyrosine is easily oxidized to form a long-lived tyrosine phenoxyl radical (33,47). Upon recombination of two tyrosyl radicals, the major product is 2,2′-bityrosine.…”

Section: Discussionmentioning

confidence: 99%

Determining Protein−Protein Interactions by Oxidative Cross-Linking of a Glycine-Glycine-Histidine Fusion Protein

Brown

Burlingame

et al. 1998

Biochemistry

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The Ni(II) complex of the tripeptide NH 2 -glycine-glycine-histidine-COOH (GGH) mediates efficient protein-protein cross-linking in the presence of oxidants such as oxone and monoperoxyphthalic acid (MMPP). Here we demonstrate that GGH fused to the amino terminus of a protein can still support cross-linking. The tripeptide was expressed at the amino terminus of ecotin, a dimeric macromolecular serine protease inhibitor found in the periplasm of Escherichia coli. In the presence of Ni(OAc) 2 and MMPP, GGH-ecotin is cross-linked to give a species that has an apparent molecular mass of a GGHecotin dimer with no observable protein degradation. The cross-linking reaction occurs between two ecotin proteins in a dimer complex. Furthermore, GGH-ecotin can be cross-linked to a serine protease target, trypsin, and the reaction is specific for proteins that interact with ecotin. The cross-linking reaction has been carried out on small peptides, and the reaction products have been analyzed by matrix-assisted laser desorption/ionization mass spectrometry. The target of the reaction is tyrosine, and the product is bityrosyl cross-links. The yield of the cross-linking is on the order of 15%. However, the reaction efficiency can be increased 4-fold by a single amino acid substitution in the carboxy terminus of ecotin that places an engineered tyrosine within 5 Å of a naturally occurring tyrosine. This cross-linking methodology allows for the protein cross-linking reagent to be encoded for at the DNA level, thus circumventing the need for posttranslational modification.

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“…Tyrosine is easily oxidized to form a long-lived tyrosine phenoxyl radical (33,47). Upon recombination of two tyrosyl radicals, the major product is 2,2′-bityrosine.…”

Section: Discussionmentioning

confidence: 99%

Determining Protein−Protein Interactions by Oxidative Cross-Linking of a Glycine-Glycine-Histidine Fusion Protein

Brown

Burlingame

et al. 1998

Biochemistry

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“…The HPLC chromatogram of the product solution (Figure 6 a) shows peaks at 15.1 (3-hydroxytyrosine, HO À Tyr), 17.1 (Tyr), and 24.0 min (NO 2 À Tyr, peaks were assigned by spiking with authentic samples). HOÀTyr is a product of the reaction of Tyr with COH, [38] the latter species produced by the homolytic decomposition of ONOOH (Scheme 1). To quantify the amount of NO 2 À Tyr and HO À Tyr formed, standard calibration curves for these two compounds were generated under the same conditions (see the Supporting Information, Figures S9 and S10).…”

mentioning

confidence: 99%

“…and CNO 2 . Furthermore, the presence or absence of the HO À Tyr product provides a convenient way to check the efficiency of the COH scavenger, because HO À Tyr is a product of the reaction of Tyr with COH [38] and should therefore not be formed if the COH scavenger scavenges all COH formed during the reaction. d-mannitol and ethanol were tested for their ability to compete with Tyr for COH in this system.…”

mentioning

confidence: 99%

Mechanistic Studies on the Reaction between Cob(II)alamin and Peroxynitrite: Evidence for a Dual Role for Cob(II)alamin as a Scavenger of Peroxynitrous Acid and Nitrogen Dioxide

Mukherjee

Brasch

2011

Chemistry A European J

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Peroxynitrite/peroxynitrous acid (ONOO(-)/ONOOH; pK(a(ONOOH)) =6.8) is implicated in multiple chronic inflammatory and neurodegenerative diseases. Both mammalian B(12)-dependent enzymes are inactivated under oxidative stress conditions. We report studies on the kinetics of the reaction between peroxynitrite/peroxynitrous acid and a major intracellular vitamin B(12) form, cob(II)alamin (Cbl(II)), using stopped-flow spectroscopy. The pH dependence of the reaction is consistent with peroxynitrous acid reacting directly with Cbl(II) to give cob(III)alamin (Cbl(III)) and (.)NO(2) , followed by a subsequent rapid reaction between (.)NO(2) and a second molecule of Cbl(II) to primarily form nitrocobalamin. In support of this mechanism, a Cbl(II)/ONOO(H) stoichiometry of 2:1 is observed at pH 7.35 and 12.0. The final major Cbl(III) product observed (nitrocobalamin or hydroxycobalamin) depends on the solution pH. Analysis of the reaction products in the presence of tyrosine-a well-established (.)NO(2) scavenger-reveals that Cbl(II) reacts with (.)NO(2) at least an order of magnitude faster than tyrosine itself. Given that protein-bound Cbl is accessible to small molecules, it is likely that enzyme-bound and free intracellular Cbl(II) molecules are rapidly oxidized to inactive Cbl(III) upon exposure to peroxynitrite or (.)NO(2).

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“…Previous experimental studies reported on OH addition on the different positions of the aromatic ring [7]. Concerning Tyr and Phe, OH may add either on C-2 or C-3 (and the symmetrical C-4 and C-5).…”

Section: Importance Of the Prototype Size On Tyr And Phe Oxidationmentioning

confidence: 99%

“…Aromatic amino acid (Tyr and Phe) OHadducts were observed by pulse radiolysis experiments, in neutral aqueous solution [2,7]. The OH radical addition was demonstrated to be the primary reaction.…”

Section: Adduct Formationmentioning

confidence: 99%

Toward understanding the protein oxidation processes: ^•OH addition on tyrosine, phenylalanine, or methionine?

Trouillas

Bergès

Houée-Levin⊥

2011

Int J of Quantum Chemistry

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Oxidation of peptides and proteins by OH radicals produced in oxidative stress or in radiotherapy, accidental irradiations, etc., is well known to form oxidative metabolites that are responsible for numerous diseases including neurodegenerative pathologies. Tyrosine (Tyr), Phenylalanine (Phe), and Methionine (Met) residues are known to be the major targets of OH radicals. This study aims at better understanding the OH addition process on these three amino acids. On the basis of different amino acid prototypes, the Gibbs energy (DG) (B3P86/6-31þG(d,p)) and rate constants (k TST ) (MPWB1K/6-31þG(d,p)) of OH addition were calculated. The OH addition capacity was studied (i) on the different positions of the aromatic rings of Tyr and Phe and (ii) on the S-atom of Met. The addition was favored on the aromatic rings of Tyr and Phe with almost the same DG addition values for both amino acids. No preferential position was found. The only parameter that may influence the OH-adduct formation is the presence or absence of intra-H bondings. In agreement with the experimental data available from the literature, the OH-adduct on Met appeared to be less favored.

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Reactivity of hydroxyl with tyrosine in aqueous solution studied by pulse radiolysis

Cited by 94 publications

References 0 publications

Determining Protein−Protein Interactions by Oxidative Cross-Linking of a Glycine-Glycine-Histidine Fusion Protein

Determining Protein−Protein Interactions by Oxidative Cross-Linking of a Glycine-Glycine-Histidine Fusion Protein

Mechanistic Studies on the Reaction between Cob(II)alamin and Peroxynitrite: Evidence for a Dual Role for Cob(II)alamin as a Scavenger of Peroxynitrous Acid and Nitrogen Dioxide

Toward understanding the protein oxidation processes: ^•OH addition on tyrosine, phenylalanine, or methionine?

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Reactivity of hydroxyl with tyrosine in aqueous solution studied by pulse radiolysis

Cited by 94 publications

References 0 publications

Determining Protein−Protein Interactions by Oxidative Cross-Linking of a Glycine-Glycine-Histidine Fusion Protein

Determining Protein−Protein Interactions by Oxidative Cross-Linking of a Glycine-Glycine-Histidine Fusion Protein

Mechanistic Studies on the Reaction between Cob(II)alamin and Peroxynitrite: Evidence for a Dual Role for Cob(II)alamin as a Scavenger of Peroxynitrous Acid and Nitrogen Dioxide

Toward understanding the protein oxidation processes: •OH addition on tyrosine, phenylalanine, or methionine?

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Toward understanding the protein oxidation processes: ^•OH addition on tyrosine, phenylalanine, or methionine?