Impact of Reactive Species on Amino Acids—Biological Relevance in Proteins and Induced Pathologies

Andrés, Celia María Curieses; Pérez de la Lastra, José Manuel; Andrés Juan, Celia; Plou, Francisco J.; Pérez-Lebeña, Eduardo

doi:10.3390/ijms232214049

Cited by 71Redox biology and oxidative stressFree Radicals and AntioxidantsAntioxidant Activity and Oxidative Stress

Impact of Reactive Species on Amino Acids—Biological Relevance in Proteins and Induced Pathologies

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Andrés, Celia María Curieses, Pérez de la Lastra, José Manuel, Andrés Juan, Celia, Plou, Francisco J., Pérez-Lebeña, Eduardo·2022·International Journal of Molecular Sciences

DOI 10.3390/ijms232214049PMC PMC9692786

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Abstract

This review examines the impact of reactive species RS (of oxygen ROS, nitrogen RNS and halogens RHS) on various amino acids, analyzed from a reactive point of view of how during these reactions, the molecules are hydroxylated, nitrated, or halogenated such that they can lose their capacity to form part of the proteins or peptides, and can lose their function. The reactions of the RS with several amino acids are described, and an attempt was made to review and explain the chemical mechanisms of the formation of the hydroxylated, nitrated, and halogenated derivatives. One aim of this work is to provide a theoretical analysis of the amino acids and derivatives compounds in the possible positions. Tyrosine, methionine, cysteine, and tryptophan can react with the harmful peroxynitrite or •OH and •NO2 radicals and glycine, serine, alanine, valine, arginine, lysine, tyrosine, histidine, cysteine, methionine, cystine, tryptophan, glutamine and asparagine can react with hypochlorous acid HOCl. These theoretical results may help to explain the loss of function of proteins subjected to these three types of reactive stresses. We hope that this work can help to assess the potential damage that reactive species can cause to free amino acids or the corresponding residues when they are part of peptides and proteins.

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Peroxynitrite can nitrate tyrosine or tryptophan residues or oxidise methionine residues.
“In addition, peroxynitrite is capable of nitrating tyrosine or tryptophan residues, or oxidising methionine residues [123,124,125,126,127,128].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [128]
HOCl oxidises tyrosine residues to form the tyrosyl radical.
“HOCl oxidises tyrosine residues to form the tyrosyl radical [128].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [128]

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Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031841 · Cited by 342 · see citing works
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Direct oxidation of boronates by peroxynitrite: Mechanism and implications in fluorescence imaging of peroxynitrite
Sikora, A., Zielonka, J., Lopez, M., Joseph, J., & Kalyanaraman, B. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.08.006 · Cited by 364 · see citing works
Loss of 3-Nitrotyrosine on Exposure to Hypochlorous Acid: Implications for the Use of 3-Nitrotyrosine as a Bio-markerin Vivo
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The critical role of reactive nitrogen species in lung ischemia reperfusion injury
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A highly selective water-soluble optical probe for endogenous peroxynitrite
Hou, J., Yang, J. P., Li, K., Liao, Y.-X., Yu, K., Xie, Y., & Yu, X. (2014) · Chemical Communications · doi:10.1039/c4cc04192e · Cited by 91 · see citing works

Authors: Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E.
Affiliations: Hospital Clínico Universitario de Valladolid (ES)
Institute of Natural Products and Agrobiology, CSIC-Spanish Research Council, Avda. Astrofísico Fco. Sánchez, 3, 38206 La Laguna, Spain
Cinquima Institute and Department of Organic Chemistry, Faculty of Sciences, Valladolid University, Paseo de Belén, 7, 47011 Valladolid, Spain
Consejo Superior de Investigaciones Científicas (ES)
Sistemas de Biotecnología y Recursos Naturales, 47625 Valladolid, Spain
ORCID: Andrés, Celia María Curieses
Pérez de la Lastra, José Manuel
Plou, Francisco J.
Venue: International Journal of Molecular Sciences
Publisher: MDPI AG
Published: 2022-11-14
Volume: 23
Issue: 22
Pages: 14049
ISSN: 1422-0067 (ISSN-L)
DOI: 10.3390/ijms232214049
PMC: PMC9692786
OpenAlex: W4309210811
Cited by: 71
References: 159
Citations by year: 2026: 21 · 2025: 18 · 2024: 24 · 2023: 8
FWCI: 1.30
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: International Journal of Molecular Sciences (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion, cc-by)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: Cooperation Program INTERREG-MAC 2014–2020, with European Funds for Regional Development-FEDER (ProID2020010134, 2019SP43, PID2019-105838RB-C31)
Agencia Canaria de Investigación, Innovación y Sociedad de la Información (ProID2020010134, 2019SP43, PID2019-105838RB-C31)
Caja Canarias (ProID2020010134, 2019SP43, PID2019-105838RB-C31)
Spanish Ministry of Economy and Competitiveness (ProID2020010134, 2019SP43, PID2019-105838RB-C31)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
Keywords: reactive species, reactive oxygen species, reactive nitrogen species, amino acid modification, protein damage, hydroxylation, nitration, halogenation, peroxynitrite, hydroxyl radicals, nitric oxide radical, hypochlorous acid, tyrosine, methionine, cysteine, tryptophan, reaction mechanism
MeSH terms: Amino Acids, Cysteine, Methionine, Proteins, Tryptophan, Tyrosine

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Impact of Reactive Species on Amino Acids—Biological Relevance in Proteins and Induced Pathologies

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