Determination of 2-oxohistidine by amino acid analysis

Lewisch, Sandra A.; Levine, Rodney L.

doi:10.1016/s0076-6879(99)00120-2

Cited by 17 publications

(22 citation statements)

References 10 publications

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“…Much higher levels of modification (41% loss) were detected by amino acid analysis, consistent with the presence of additional products that were not detected in the MS analysis. The number of known modifications to His residues is significant [7][8][9][10][11][12][13][14], and most databases of posttranslational modifications do not include cross-linked products [37], thereby presenting significant challenges to obtaining a material balance between parent loss and product formation for this residue. The high level of modification of His is however consistent with the known high rate constant for reaction of 1 O 2 with this amino acid [50].…”

Section: Discussionmentioning

confidence: 99%

“…It is known that Tyr oxidation can result in sidechain modifications with formation of both oxidized species such as 3,4-dihydroxyphenylalanine (DOPA and the corresponding quinone), and cross-links via the formation of dityrosine (diTyr) [6]. The chemistry of His oxidation is complex, but evidence has been presented for the formation of 2-oxo-His as initial intermediates which can undergo ring opening and further degradation [7,8], resulting in a large range of products [9][10][11][12]. Evidence has also been presented for a role of His residues in cross-linking, either via His-His linkages [9][10][11]13], or as a result of reaction of oxidized His species with nucleophiles e.g.…”

Section: Introductionmentioning

confidence: 99%

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Structural and functional changes in RNAse A originating from tyrosine and histidine cross-linking and oxidation induced by singlet oxygen and peroxyl radicals

Leinisch

Mariotti

Hägglund

et al. 2018

Free Radical Biology and Medicine

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Oxidation can be induced by multiple processes in biological samples, with proteins being important targets due to their high abundance and reactivity. Oxidant reactions with proteins are not comprehensively understood, but it is known that structural and functional changes may be a cause, or a consequence, of disease. The mechanisms of oxidation of the model protein RNAse A by singlet oxygen (O) were examined and compared to peroxyl radical (ROO) oxidation, both common biological oxidants. This protein is a prototypic member of the RNAse family that exhibits antiviral activity by cleaving single-stranded RNA. RNAse A lacks tryptophan and cysteine residues which are major oxidant targets, but contains multiple histidine, tyrosine and methionine residues; these were therefore hypothesized to be the major sites of damage. O and ROO induce different patterns and extents of damage; both induce cross-links and side-chain oxidation, and O exposure modulates enzymatic activity. Multiple products have been characterized including methionine sulfoxide and sulfone, alcohols, DOPA, 2-oxohistidine, histidine-derived ring-opened species and inter- and intra-molecular cross-links (di-tyrosine, histidine-lysine, histidine-arginine, tyrosine-lysine). In addition to methionine modification, which appears not to be causative to activity loss, singlet oxygen also induces alteration to specific histidine, tyrosine and proline residues, including modification and cross-linking of the active site histidine, His12. The high homology among the RNAse family suggests that similar modifications may occur in humans, and be associated with the increased risk of viral infections in people with diabetes, as markers for O have been found in early stages of this pathology.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Structural and functional changes in RNAse A originating from tyrosine and histidine cross-linking and oxidation induced by singlet oxygen and peroxyl radicals

Leinisch

Mariotti

Hägglund

et al. 2018

Free Radical Biology and Medicine

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“…This reaction, which forms imidazolone, is known to occur in histidine-containing peptides under oxidizing conditions. [23][24][25] This reaction has also been identified as a necessary step in the cross-linking of crystallins under oxidizing conditions. 26 The resulting imidazolone ring can be modified in several different ways, resulting in 2(3H)-, 2(5H)-, or 4(5H)-imidazolone.…”

Section: Discussionmentioning

confidence: 99%

“…The following discussion will center on the 2-imidazolone form because it has been observed in peptides. [23][24][25] Once the imidazolone derivative has been formed by oxidation, it is susceptible to a nucleophilic attack by one of the nitrogens in a protamine arginine side chain guanidino group. The final step in this tentative cross-linking mechanism is a further oxidation, as shown at the bottom of Figure 6.…”

Section: Discussionmentioning

confidence: 99%

A Novel Protein Cross-Linking Reaction in Stressed Neutral Protamine Hagedorn Formulations of Insulin

Beavis

Kneirman

Sharknas

et al. 1999

Journal of Pharmaceutical Sciences

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The covalent insulin-protamine product molecules formed by heat stress in Neutral Protamine Hagedorn formulations of insulin and the insulin analogue [LysB28,ProB29] were examined by mass spectrometry. The results demonstrated that the covalent cross-link between insulin and protamine was not caused by linkage through the protamine N-terminal amino group, as had been previously thought. Our results indicate that the linkage was formed between the side chain of a protamine arginine and a histidine in the insulin B chain, resulting in a net mass change of -5 Da, compared to the sum of the protamine and insulin molecular masses. A mechanism for this new type of covalent cross-linking reaction is proposed.

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“…Free radical attack on proteins results in a variety of products ( Fig. 2c,d) which include methionine sulfoxide (Ferguson and Burke, 1994) and 2-oxohistidine (Lewisch and Levine, 1995). However, protein damage is usually estimated as the total content of carbonyl groups (Fig.…”

Section: Protein Damagementioning

confidence: 99%

Untitled

1998

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Iron has a pivotal and dual role in free radical chemistry in all organisms. On the one hand, free Fe can participate in Fenton reactions and catalyze ('catalytic Fe') the generation of hydroxyl radical and other toxic oxygen species. On the other hand, Fe is a constituent of the antioxidant enzymes catalase, ascorbate peroxidase, guaiacol peroxidase, and ferro-superoxide dismutase. Protein Fe is Fenton inactive but can be released from proteins upon attack by activated oxygen.Healthy, unstressed plants avoid the interaction of catalytic Fe and peroxides by disposing of Fe in vacuoles and apoplast, by sequestering Fe in ferritin, and by having high levels of antioxidant enzymes in most subcellular compartments.However, when plants are exposed to a variety of adverse conditions, including chilling, high light, drought and paraquat, oxidative stress ensues due primarily to the decrease in antioxidant defenses but also to the increase in free radical production mediated by catalytic Fe. The latter accumulates in many stressed plant tissues. Oxidative stress may lead to metabolic dysfunction and ultimately to plant cell death, so it needs to be estimated conveniently by quantifying the oxidation products of lipids (malondialdehyde and other cytotoxic aldehydes), proteins (total carbonyls, methionine sulfoxide, 2-oxohistidine), and DNA (8-hydroxyguanine, 5hydroxycytosine). Protein oxidation appears to be a more sensitive and precocious marker than is lipid peroxidation, and DNA damage may also prove to be a useful marker for stress studies in plants.Abbreviations: MDA -malondialdehyde, SOD -superoxide dismutase, TBA -2thiobarbituric acid, TBARS -thiobarbituric acid-reactive substances.

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Determination of 2-oxohistidine by amino acid analysis

Cited by 17 publications

References 10 publications

Structural and functional changes in RNAse A originating from tyrosine and histidine cross-linking and oxidation induced by singlet oxygen and peroxyl radicals

Structural and functional changes in RNAse A originating from tyrosine and histidine cross-linking and oxidation induced by singlet oxygen and peroxyl radicals

A Novel Protein Cross-Linking Reaction in Stressed Neutral Protamine Hagedorn Formulations of Insulin

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