Oxidation of amino acids and peptides in reaction with myeloperoxidase, chloride and hydrogen peroxide

Drożdż, Ryszard; Naskalski, J; Sznajd, J

doi:10.1016/0167-4838(88)90155-0

Cited by 59 publications

(36 citation statements)

References 9 publications

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“…Reflectron TOF-MS of Asp-N digest products indicated intense ions with m/z 1457.61, 2287.98, 2448.30 (Fig. 2D), identical to the protonated peptides A8 Ϫ2-12 , A8 [13][14][15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30][31] , and Met(O)-A8 . No peptide corresponding to A8 32-57 was evident, although there was an additional ion at m/z 3802.7562.…”

Section: Resultsmentioning

confidence: 99%

“…The respiratory burst produces superoxide anion (up to 40 mol/10 6 cells) corresponding to a maximal blood concentration of ϳ200 M, which dismutates to hydrogen peroxide (H 2 O 2 ) and is converted by myeloperoxidase (MPO) to the powerful twoelectron (non-radical) oxidant hypochlorous acid (HOCl) that can modify proteins and lipids and kill invading pathogens (25,26). Reagent and MPO-generated HOCl react identically (27)(28)(29), and protein thiols and Met are preferred substrates (30). HOCl also initiates low density lipoprotein lipid peroxidation * This work was supported in part by grants from the National Health and Medical Research Council of Australia and Australian Research Council.…”

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confidence: 99%

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Novel Intra- and Inter-molecular Sulfinamide Bonds in S100A8 Produced by Hypochlorite Oxidation

Raftery

Yang

Valenzuela

et al. 2001

Journal of Biological Chemistry

122

132

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Hypochlorite is a major oxidant generated when neutrophils and macrophages are activated at inflammatory sites, such as in atherosclerotic lesions. Murine S100A8 (A8) is a major cytoplasmic protein in neutrophils and is secreted by macrophages in response to inflammatory stimuli. After incubation with reagent HOCl for 10 min, ϳ85% of A8 was converted to 4 oxidation products, with electrospay ionization mass spectrometry masses of m/z 10354, 10388, 10354 ؎ 1, and 20707 ؎ 3. All were resistant to reduction by dithiothreitol.

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

Novel Intra- and Inter-molecular Sulfinamide Bonds in S100A8 Produced by Hypochlorite Oxidation

Raftery

Yang

Valenzuela

et al. 2001

Journal of Biological Chemistry

122

132

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“…The respiratory burst produces superoxide anions which dismutate to hydrogen peroxide (H 2 O 2 ) that is converted by myeloperoxidase (MPO) and Cl Ϫ to the powerful twoelectron (non-radical) oxidant hypochlorous acid (HOCl), which can chemically modify lipids, proteins and kill invading pathogens [14]. MPO-generated and exogenous HOCl react identically [15][16][17] and protein thiols and Met are preferred substrates [18]. HOCl also initiates LDL lipid peroxidation and formation of 3-chlorotyrosine and dityrosine [19].…”

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confidence: 99%

Electrospray low energy CID and MALDI PSD fragmentations of protonated sulfinamide cross-linked peptides

Raftery

Geczy

2002

J. Am. Soc. Mass Spectrom.

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Murine S100A8 (A8) is a major cytoplasmic neutrophil protein and is converted to novel oxidation products containing Cys-amino-Lys sulfinamide cross-links and Met-sulfoxide by the neutrophil oxidant HOCl. Seven products were separated using RP-HPLC, with electrospray ionization mass spectrometry (ESI-MS) masses after deconvolution of 10,354, 10,388, Ϯ1, and 20,707, Ϯ3 Da, and all were resistant to reduction by dithiothreitol. The major products with masses of 10,354 Da contained Cys 41 -Lys 34/35 intramolecular cross-links. Additional isomeric products with identical masses (10,354 Da) were isolated and peptide mapping and ESI/MS indicated that Cys 41 forms covalent sulfinamide cross-links with either Lys 6 , Lys 76 , Lys 83 , or Lys 87 present in A8. Electrospray low energy collisionally induced (CID) spectra of multiply-charged AspN digest peptides with sulfinamide cross-links contained characteristic fragmentations that corresponded to simple cleavage of the nitrogen™sulfur bond with charge retention on either of the fragment ions, allowing conformation of cross-linked peptides. Matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) post source decay spectra of [M ϩ H] ϩ ions of the same sulfinamide-containing cross-linked peptides fragment similarly, but additional facile fragmentation reactions corresponding to formation of a protonated peptide containing de-hydroalanine were attributed to cleavage of the carbon™sulfur bond. In addition, lose of methanesulfenic acid from Met-sulfoxide was observed. A sulfinamide-containing adduct was isolated after incubation of the A8/HOCl reaction mixture with Lys or ␣ N-acetyl Lys with masses of 10,500 or 10,542 Da. ESI/MS/MS and MALDI/ post decay source (PSD) analysis of A8 32-57 -sulfinamide showed the same characteristic fragmentations as those in the sulfinamide cross-linked peptides, confirming the Cys 41 -Lys sulfinamide cross-link and suggesting that peptide-peptide sulfinamides may all fragment similarly, allowing ready identification of these cross-links in proteins from more complex biological materials. (J Am Soc Mass Spectrom 2002, 13, 709 -718)

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“…Free amino and thiol groups of amino acids and peptides constitute important targets for HOCl, yielding unstable chloramines and sulfenyl chloride intermediates, respectively (14)(15)(16). Chloramine intermediates are also detected in the reaction of HOCl with exocyclic (RNH 2 ) and heterocyclic (RNHR) amine functions in DNA bases (14,17).…”

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confidence: 99%

Linoleic acid hydroperoxide reacts with hypochlorous acid, generating peroxyl radical intermediates and singlet molecular oxygen

Miyamoto

Martinez²,

Rettori³

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

123

108

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The reaction of hypochlorous acid (HOCl) with hydrogen peroxide is known to generate stoichiometric amounts of singlet molecular oxygen [O2 ( 1 ⌬g)]. This study shows that HOCl can also react with linoleic acid hydroperoxide (LAOOH), generating O2 ( 1 ⌬g) with a yield of 13 ؎ 2% at physiological pH. Characteristic light emission at 1,270 nm, corresponding to O2 ( 1 ⌬g) monomolecular decay, was observed when HOCl was reacted with LAOOH or with liposomes containing phosphatidylcholine hydroperoxides, but not with cumene hydroperoxide or tert-butyl hydroperoxide. The generation of O2 ( 1 ⌬g lipid hydroperoxides ͉ mass spectrometry ͉ myeloperoxidase ͉ near-infrared emission ͉ 18 O-labeled oxygen

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Oxidation of amino acids and peptides in reaction with myeloperoxidase, chloride and hydrogen peroxide

Cited by 59 publications

References 9 publications

Novel Intra- and Inter-molecular Sulfinamide Bonds in S100A8 Produced by Hypochlorite Oxidation

Novel Intra- and Inter-molecular Sulfinamide Bonds in S100A8 Produced by Hypochlorite Oxidation

Electrospray low energy CID and MALDI PSD fragmentations of protonated sulfinamide cross-linked peptides

Linoleic acid hydroperoxide reacts with hypochlorous acid, generating peroxyl radical intermediates and singlet molecular oxygen

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