Determination of 2-Oxohistidine by Amino Acid Analysis

Lewisch, Sandra A.; Levine, Rodney L.

doi:10.1006/abio.1995.9974

Cited by 56 publications

(26 citation statements)

References 13 publications

(8 reference statements)

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“…The sample was centrifuged at 15,000 rpm for 10 min. The precipitate was hydrolyzed in the presence of 100 mM DTT, and the hydrolysate was analyzed by reverse-phase HPLC after o-phthalaldehyde derivatization as described (19). A standard of pure benzoyl-oxohistidine was used as control.…”

Section: Discussionmentioning

confidence: 99%

“…This treatment converts methionine to homoserine, which is detected partially as such and partially as homoserine lactone after acid hydrolysis, whereas methionine sulfoxide and other products of methionine oxidation are not affected by the reaction, reverting to methionine during acid hydrolysis, and are detected as such. Oxohistidine, unstable under typical analytical conditions, was detected in hydrolysates prepared in the presence of 100 mM DTT as described (19).…”

Section: Methodsmentioning

confidence: 99%

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Copper-catalyzed oxidation of the recombinant SHa(29–231) prion protein

Requena

Groth

Legname

et al. 2001

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

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144

115

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Metal-catalyzed oxidation may result in structural damage to proteins and has been implicated in aging and disease, including neurological disorders such as Alzheimer's disease and amyotrophic lateral sclerosis. The selective modification of specific amino acid residues with high metal ion affinity leads to subtle structural changes that are not easy to detect but may have dramatic consequences on physical and functional properties of the oxidized protein molecules. PrP contains a histidine-rich octarepeat domain that binds copper. Because copper-binding histidine residues are particularly prone to metal-catalyzed oxidation, we investigated the effect of this reaction on the recombinant prion protein SHaPrP(29 -231). Using Cu 2؉ ͞ascorbate, we oxidized SHaPrP(29 -231) in vitro. Oxidation was demonstrated by liquid chromatography͞mass spectrometry, which showed the appearance of protein species of higher mass, including increases in multiples of 16, characteristic of oxygen incorporation. Digestion studies using Lys C indicate that the 29 -101 region, which includes the histidinecontaining octarepeats, is particularly affected by oxidation. Oxidation was time-and copper concentration-dependent and was evident with copper concentrations as low as 1 M. Concomitant with oxidation, SHaPrP(29 -231) suffered aggregation and precipitation, which was nearly complete after 15 min, when the prion protein was incubated at 37°C with a 6-fold molar excess of Cu 2؉ . These findings indicate that PrP, a copper-binding protein, may be particularly susceptible to metal-catalyzed oxidation and that oxidation triggers an extensive structural transition leading to aggregation.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Copper-catalyzed oxidation of the recombinant SHa(29–231) prion protein

Requena

Groth

Legname

et al. 2001

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

Self Cite

144

115

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“…Many studies have reported that 2-oxohistidine residue had been found in various peptides and proteins (16,(43)(44)(45)(46)(47)(48)(49)(50)(51). To identify proteins which may bind specifically to 2-oxohistidine residue, we devised an experimental strategy illustrated in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Histidine is highly susceptible to ROS damage, because it has strong metal chelation affinity and often constitutes the binding site for metal ions (14,15). The presence of H 2 O 2 and redox-active metals (Cu and Fe) can lead to metal-catalyzed oxidation (MCO, also called Fenton-type chemistry), which converts histidine side chain to 2-oxohistidine (16,17).…”

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confidence: 99%

Identification of 2-oxohistidine Interacting Proteins Using E. coli Proteome Chips

Lin

Tsai

Liu

et al. 2016

Molecular & Cellular Proteomics

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Cellular proteins are constantly damaged by reactive oxygen species generated by cellular respiration. Because of its metal-chelating property, the histidine residue is easily oxidized in the presence of Cu/Fe ions and H 2 O 2 via metal-catalyzed oxidation, usually converted to 2-oxohistidine. We hypothesized that cells may have evolved antioxidant defenses against the generation of 2-oxohistidine residues on proteins, and therefore there would be cellular proteins which specifically interact with this oxidized side chain. Using two chemically synthesized peptide probes containing 2-oxohistidine, high-throughput interactome screening was conducted using the E. coli K12 proteome microarray containing >4200 proteins. Ten interacting proteins were identified, and successfully validated using a third peptide probe, fluorescence polarization assays, as well as binding constant measurements. We discovered that 9 out of 10 identified proteins seemed to be involved in redox-related cellular functions. We also built the functional interaction network to reveal their interacting proteins. The network showed that our interacting proteins were enriched in oxido-reduction processes, ion binding, and carbon metabolism. A consensus motif was identified among these 10 bacterial interacting proteins based on bioinformatic analysis, which also appeared to be present on human S100A1 protein. Besides, we found that the consensus binding motif among our identified proteins, including bacteria and human, were located within ␣-helices and faced the outside of proteins. The combination of chemically engineered peptide probes with proteome microarrays proves to be an efficient discovery platform for protein interactomes of unusual post-translational modifications, and sensitive enough to detect even the insertion of a single oxygen atom in this case.

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“…It became known that the cytosolic SOD, Cu,ZnSOD (also known as SOD1) suffers oxidative modification by its product, hydrogen peroxide, a reaction potentially involving site-specifically formed hydroxyl radicals at the active site containing redox-active Cu II (Uchida & Kawakishi, 1994). This process leads to the formation of 2-oxo-His (structure 5), a characteristic product identified also for the in vitro metalcatalyzed oxidation of other proteins (Lewisch & Levine, 1995;Zhao et al, 1997). Interestingly, recent tandem mass spectrometry data show that for Cu,ZnSOD not the His residue bridging the redox-active Cu II and the structurally important Zn II ion is oxidized, but His residues only binding Cu II represent the predominant oxidation targets (Kurahashi et al, 2001).…”

Section: Cuzn Superoxide Dismutasementioning

confidence: 93%

Mass spectrometry in aging research

Schöneich

2004

Mass Spectrometry Reviews

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This review covers the application of mass spectrometric techniques to aging research. Modern proteomic strategies will be discussed as well as the targeted analysis of specific proteins for the correlation of post-translational modifications with protein function. Selected examples will show both the power and also current limitations of the respective techniques. Experimental results and strategies are discussed in view of current theories of the aging process. # 2004 Wiley Periodicals, Inc., Mass Spec Rev 24: [701][702][703][704][705][706][707][708][709][710][711][712][713][714][715][716][717][718] 2005

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Determination of 2-Oxohistidine by Amino Acid Analysis

Cited by 56 publications

References 13 publications

Copper-catalyzed oxidation of the recombinant SHa(29–231) prion protein

Copper-catalyzed oxidation of the recombinant SHa(29–231) prion protein

Identification of 2-oxohistidine Interacting Proteins Using E. coli Proteome Chips

Mass spectrometry in aging research

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