ArticleProtein science : a publication of the Protein Society2006
3-Nitrotyrosine as a spectroscopic probe for investigating protein protein interactions.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 70 citations in OpenAlex.
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- Non-Canonical Amino Acids in Analyses of Protease Structure and Function.International journal of molecular sciences · 2023Review
- Tyrosine Nitroxidation Does Not Affect the Ability of α-Synuclein to Bind Anionic Micelles, but It Diminishes Its Ability to Bind and Assemble Synaptic-like Vesicles.Antioxidants (Basel, Switzerland) · 2023Article
- Photochemical synthesis of pink silver and its use for monitoring peptide nitration via surface enhanced Raman spectroscopy (SERS).Amino acids · 2022Article
- Sporicidal Action of Pulsed Radiation of Hot Plasma.Sovremennye tekhnologii v meditsine · 2022Article
- Insights Into the Mechanism of Tyrosine Nitration in Preventing β-Amyloid Aggregation in Alzheimer's Disease.Frontiers in molecular neuroscience · 2021Article
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- Dissecting Optical Response and Molecular Structure of Fluorescent Proteins With Non-canonical Chromophores.Frontiers in molecular biosciences · 2020Article
- Design of a Protein Motif Responsive to Tyrosine Nitration and an Encoded Turn-Off Sensor of Tyrosine Nitration.Biochemistry · 2019Article
- Tyrosine-Nitrated Proteins: Proteomic and Bioanalytical Aspects.Antioxidants & redox signaling · 2017Review
- Loop Electrostatics Asymmetry Modulates the Preexisting Conformational Equilibrium in Thrombin.Biochemistry · 2016Article
- Mechanism of glyceraldehyde-3-phosphate dehydrogenase inactivation by tyrosine nitration.Protein science : a publication of the Protein Society · 2010Article
- Electron capture dissociation mass spectrometry of tyrosine nitrated peptides.Journal of the American Society for Mass Spectrometry · 2010Article
- Chemoselective nitration of phenols with tert-butyl nitrite in solution and on solid support.Organic letters · 2009Article
- High-throughput liquid-liquid fractionation of multiple protein post-translational modifications.Journal of proteome research · 2009Article
- Smart Polymeric Gels: Redefining the Limits of Biomedical Devices.Progress in polymer science · 2007Article
- o-Nitrotyrosine and p-iodophenylalanine as spectroscopic probes for structural characterization of SH3 complexes.Protein science : a publication of the Protein Society · 2007Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
3-Nitrotyrosine (NT) is approximately 10(3)-fold more acidic than Tyr, and its absorption properties are strongly pH-dependent. NT absorbs radiation in the wavelength range where Tyr and Trp emit fluorescence (300-450 nm), and it is essentially nonfluorescent. Therefore, NT may function as an energy acceptor in resonance energy transfer (FRET) studies for investigating ligand protein interactions. Here, the potentialities of NT were tested on the hirudin thrombin system, a well-characterized protease inhibitor pair of key pharmacological importance. We synthesized two analogs of the N-terminal domain (residues 1-47) of hirudin: Y3NT, in which Tyr3 was replaced by NT, and S2R/Y3NT, containing the substitutions Ser2 --> Arg and Tyr3 --> NT. The binding of these analogs to thrombin was investigated at pH 8 by FRET and UV/Vis-absorption spectroscopy. Upon hirudin binding, the fluorescence of thrombin was reduced by approximately 50%, due to the energy transfer occurring between the Trp residues of the enzyme (i.e., the donors) and the single NT of the inhibitor (i.e., the acceptor). The changes in the absorption spectra of the enzyme inhibitor complex indicate that the phenate moiety of NT in the free state becomes protonated to phenol in the thrombin-bound form. Our results indicate that the incorporation of NT can be effectively used to detect protein protein interactions with sensitivity in the low nanomolar range, to uncover subtle structural features at the ligand protein interface, and to obtain reliable Kd values for structure activity relationship studies. Furthermore, advances in chemical and genetic methods, useful for incorporating noncoded amino acids into proteins, highlight the broad applicability of NT in biotechnology and pharmacological screening.
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