{"title":"Special issue on “Peroxynitrite and Reactive Nitrogen Species” dedicated to the 25th anniversary of the nitric oxide Nobel Prize","authors":"Ari Zeida, Jacek Zielonka, Madia Trujillo","doi":"10.1016/j.rbc.2024.100044","DOIUrl":"10.1016/j.rbc.2024.100044","url":null,"abstract":"","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"10 ","pages":"Article 100044"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143153420","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Monika Rola , Jacek Zielonka , Renata Smulik-Izydorczyk , Jakub Pięta , Karolina Pierzchała , Adam Sikora , Radosław Michalski
{"title":"Boronate-based bioactive compounds activated by peroxynitrite and hydrogen peroxide","authors":"Monika Rola , Jacek Zielonka , Renata Smulik-Izydorczyk , Jakub Pięta , Karolina Pierzchała , Adam Sikora , Radosław Michalski","doi":"10.1016/j.rbc.2024.100040","DOIUrl":"10.1016/j.rbc.2024.100040","url":null,"abstract":"<div><p>Boronates react directly and stoichiometrically with peroxynitrite and hydrogen peroxide. For this reason, boronates have been widely used as peroxynitrite- and hydrogen peroxide-sensitive moieties in various donors of bioactive compounds. So far, numerous boronate-based prodrugs and theranostics have been developed, characterized, and used in biological research. Here, the kinetic aspects of their activation are discussed, and the potential benefits of modifying their original structure with a boronic or boronobenzyl moiety are described.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"10 ","pages":"Article 100040"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S277317662400021X/pdfft?md5=c58c101adf9a9f3d95e787fad55df43b&pid=1-s2.0-S277317662400021X-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142096129","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ann-Kathrin Weishaupt , Anna Gremme , Torben Meiners , Vera Schwantes , Karsten Sarnow , Alicia Thiel , Tanja Schwerdtle , Michael Aschner , Heiko Hayen , Julia Bornhorst
{"title":"Dysfunctional copper homeostasis in Caenorhabditis elegans affects genomic and neuronal stability","authors":"Ann-Kathrin Weishaupt , Anna Gremme , Torben Meiners , Vera Schwantes , Karsten Sarnow , Alicia Thiel , Tanja Schwerdtle , Michael Aschner , Heiko Hayen , Julia Bornhorst","doi":"10.1016/j.rbc.2024.100043","DOIUrl":"10.1016/j.rbc.2024.100043","url":null,"abstract":"<div><div>While copper (Cu) is an essential trace element for biological systems due to its redox properties, excess levels may lead to adverse effects partly due to overproduction of reactive species. Thus, a tightly regulated Cu homeostasis is crucial for health. Cu dyshomeostasis and elevated labile Cu levels are associated with oxidative stress and neurodegenerative disorders, but the underlying mechanisms have yet to be fully characterized. Here, we used <em>Caenorhabditis elegans</em> loss-of-function mutants of the Cu chaperone ortholog atox-1 and the Cu binding protein ortholog ceruloplasmin to model Cu dyshomeostasis, as they display a shifted ratio of total Cu towards labile Cu. We applied highly selective and sensitive techniques to quantify metabolites associated to oxidative stress with focus on mitochondrial integrity, oxidative DNA damage and neurodegeneration all in the context of a disrupted Cu homeostasis. Our novel data reveal elevated oxidative stress, compromised mitochondria displaying reduced ATP levels and cardiolipin content. Cu dyshomeostasis further induced oxidative DNA damage and impaired DNA damage response as well as neurodegeneration characterized by behavior and neurotransmitter analysis. Our study underscores the essentiality of a tightly regulated Cu homeostasis as well as mitochondrial integrity for both genomic and neuronal stability.</div></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"10 ","pages":"Article 100043"},"PeriodicalIF":0.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142534424","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"NADPH oxidase 5: Where are we now and which way to proceed?","authors":"Gábor L. Petheő, Zsolt Szeles, Miklós Geiszt","doi":"10.1016/j.rbc.2024.100036","DOIUrl":"10.1016/j.rbc.2024.100036","url":null,"abstract":"<div><p>Since the incorporation of mitochondria in early eukaryotes cells struggle to keep the deleterious effects of reactive oxygen species (ROS), mainly originating from the respiratory chain, at bay. Evolutionary adaptation to ROS burden went so far that by acting as messenger and effector molecules, ROS became important in maintaining homeostasis. The evolutionary success of this phenomenon is underscored by the arising of professional ROS-generating enzymes, namely the family of NADPH oxidases (NOXes). NOXes, by shaping ROS levels at different subcellular locations and in extracellular space, are involved in such fundamental functions as proliferation, differentiation, apoptosis, host defense, fertilization, and hormone biosynthesis. NOX5, being a calcium-regulated professional ROS source exerts its function at the crossroad of these two fundamental but potentially deleterious intracellular signaling pathways (i.e. Ca<sup>2+</sup> and ROS). The expression of NOX5 in the adult human body under unchallenged conditions is restricted to very few sites, among which the two major tissue groups are genital organs (mainly testis) and immune tissues (mainly spleen). In cases of increased cellular proliferation and protein synthesis (e.g., diverse tumors, cultured primary cells, or sites of tissue damage) the expression and activity of NOX5 is often upregulated in various tissues. This and the evolutionary conserved nature of NOX5 would imply a very fundamental role for this enzyme, but intriguingly the genomes of rodents essentially lack the NOX5 gene. The latter fact had been a major obstacle in determining the physiological roles of NOX5 in normal tissues until the very recent generation of a NOX5-deficient rabbit model.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"9 ","pages":"Article 100036"},"PeriodicalIF":0.0,"publicationDate":"2024-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2773176624000178/pdfft?md5=2687164805394d26bf3476b55ab647bc&pid=1-s2.0-S2773176624000178-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141849241","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Andresa Messias , Aníbal Rauber , Sofía Vuletich , Ari Zeida , Jonathan A. Semelak , Darío A. Estrin
{"title":"Comparing thiol and selenol reactivity towards peroxynitrite by computer simulation","authors":"Andresa Messias , Aníbal Rauber , Sofía Vuletich , Ari Zeida , Jonathan A. Semelak , Darío A. Estrin","doi":"10.1016/j.rbc.2024.100035","DOIUrl":"10.1016/j.rbc.2024.100035","url":null,"abstract":"<div><p>Peroxynitrite is a very reactive species implicated in a variety of pathophysiological cellular processes. Particularly, peroxynitrite-mediated oxidation of cellular thiol-containing compounds such as cysteine residues is a key process which has been extensively studied. Cysteine plays roles in many redox biochemistry pathways. In contrast, selenocysteine, the 21st amino acid, is only present in 25 human proteins. Investigating the molecular basis of selenocysteine's reactivity may provide insights into its unique role in these selenocysteine-containing proteins. The two-electron oxidation of thiols or selenols by peroxynitrite is a process that is carried out by the thiolate/selenate forms and peroxynitrous acid.</p><p>In this work, we shed light on the molecular basis of the differential reactivity of both species towards peroxynitrite by means of state-of-the-art computer simulations. We performed electronic structure calculations of the reaction in the methanethiolate and methaneselenolate model systems with peroxynitrous acid at different levels of theory using an implicit solvent scheme. In addition, we employed a multi-scale quantum mechanics/molecular mechanics approach for obtaining free energy profiles of these chemical reactions in aqueous solution, which enabled the comparison between the simulations and the available experimental data. Our results suggest that the larger reactivity observed in the selenocysteine case at physiological pH is mainly due to the lower pKa, which affords a larger fraction of the reactive anionic species in these conditions, and in a second place to a slightly enhanced intrinsic reactivity of the selenate form due to its larger nucleophilicity.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"9 ","pages":"Article 100035"},"PeriodicalIF":0.0,"publicationDate":"2024-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2773176624000166/pdfft?md5=b9af632f0685ee493c0ed788423b63f7&pid=1-s2.0-S2773176624000166-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141850730","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Nicole Colussi , Fei Chang , Francisco J. Schopfer
{"title":"The specificity of endogenous fatty acid nitration: only conjugated substrates support the in vivo formation of nitro-fatty acids","authors":"Nicole Colussi , Fei Chang , Francisco J. Schopfer","doi":"10.1016/j.rbc.2024.100037","DOIUrl":"10.1016/j.rbc.2024.100037","url":null,"abstract":"<div><p>Through multiple pathways, nitrogen dioxide (•NO<sub>2</sub>) is the main species involved in endogenous nitration reactions. Early studies in the field primarily explored tyrosine nitration, a dominant reaction in the field. It was later shown that lipids are also nitration targets and generate an array of reaction products. Conjugated fatty acids are the preferential substrates of lipid nitration in vivo, generating electrophilic nitro-fatty acids (NO<sub>2</sub>–FAs), which serve as pleiotropic signaling modulators. In contrast, exposure of bisallylic fatty acids, including linoleic, linolenic and arachidonic acid, to •NO<sub>2</sub> does not lead, under biological conditions, to the formation of nitrated species. This review focuses on the reaction mechanisms and products of lipid nitration and substrate specificity, focusing on the differential reactivity of conjugated dienes and bisallylic alkenes.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"9 ","pages":"Article 100037"},"PeriodicalIF":0.0,"publicationDate":"2024-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S277317662400018X/pdfft?md5=96e201513036acdcd04293b5d3e95639&pid=1-s2.0-S277317662400018X-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141853118","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Diffusion of peroxynitrite, its precursors, and derived reactive species, and the effect of cell membranes","authors":"Matías N. Möller, Ana Denicola","doi":"10.1016/j.rbc.2024.100033","DOIUrl":"10.1016/j.rbc.2024.100033","url":null,"abstract":"<div><p>Peroxynitrite is a powerful oxidant formed in vivo in sites where superoxide and nitric oxide coincide. Peroxynitrite is cytotoxic through oxidative modification of target biomolecules that can occur by direct or indirect reactions. Indirect reactions usually involve the generation of peroxynitrite-derived radicals that include nitrogen dioxide, hydroxyl radical, and carbonate radical. All these species have different behaviors in vivo, because of their intrinsic reactivity and how effectively they can be compartmentalized by cellular membranes. In this review, we analyze quantitative information on the estimated half-lives and the corresponding estimated diffusion distances of peroxynitrite, its precursors, and its derived reactive species in vivo. Furthermore, we discuss the permeability of cellular and synthetic lipid membranes to the different species and how effective compartmentalization is achieved for some of them, limiting the biological site of reactions.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"9 ","pages":"Article 100033"},"PeriodicalIF":0.0,"publicationDate":"2024-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2773176624000142/pdfft?md5=330518d6b68fea24fff7146d2022ce23&pid=1-s2.0-S2773176624000142-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141629868","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Renata Smulik-Izydorczyk , Jakub Pięta , Radosław Michalski , Monika Rola , Karol Kramkowski , Angelika Artelska , Jacek Zielonka , Adam Bartłomiej Sikora
{"title":"The chemistry of HNO-releasing compounds","authors":"Renata Smulik-Izydorczyk , Jakub Pięta , Radosław Michalski , Monika Rola , Karol Kramkowski , Angelika Artelska , Jacek Zielonka , Adam Bartłomiej Sikora","doi":"10.1016/j.rbc.2024.100031","DOIUrl":"10.1016/j.rbc.2024.100031","url":null,"abstract":"<div><p><strong>HNO</strong> (azanone or nitroxyl), formally a product of the one-electron reduction of a nitric oxide, exhibits diverse and unique biological activity. The chemistry, biochemistry, and biological/pharmacological effects of <strong>H</strong><strong>N</strong><strong>O</strong> have been studied extensively. Due to rapid dimerization and hence short lifetime in solutions, in chemical and biological studies <strong>HNO</strong> is typically produced <em>in situ</em> from its thermal donors. To date, a great variety of chemical <strong>HNO</strong> donors have been synthesized, characterized, and utilized in biological studies. Here, we discuss the chemistry of <strong>HNO</strong>-releasing compounds, with the emphasis on the complexity of the proposed reaction mechanisms.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"8 ","pages":"Article 100031"},"PeriodicalIF":0.0,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2773176624000129/pdfft?md5=d41d616194237ca22b5077ab1b087f18&pid=1-s2.0-S2773176624000129-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141281040","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Protein tyrosine nitration","authors":"Harry Ischiropoulos","doi":"10.1016/j.rbc.2024.100030","DOIUrl":"10.1016/j.rbc.2024.100030","url":null,"abstract":"<div><p>Protein tyrosine nitration is a post-translational modification originating from the biological chemistry of nitric oxide. This article highlights key milestones, discusses apparent controversies and perspectives that have emerged in the last 35 years of research on protein tyrosine nitration. Since the execution of nitric oxide signaling is accomplished entirely by protein post translational modifications (PTMs), the prospect that protein tyrosine nitration augments nitric oxide signaling remains an intriguing but incomplete concept deserving further consideration.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"8 ","pages":"Article 100030"},"PeriodicalIF":0.0,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2773176624000117/pdfft?md5=9354ac441d5bfc4d3d9c04f3f6b7c502&pid=1-s2.0-S2773176624000117-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141232253","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ana G. Sánchez, Deborah J. Keszenman, R. Daniel Peluffo
{"title":"Purine, nucleoside, and DNA nitration by peroxynitrite: Mechanistic considerations","authors":"Ana G. Sánchez, Deborah J. Keszenman, R. Daniel Peluffo","doi":"10.1016/j.rbc.2024.100028","DOIUrl":"10.1016/j.rbc.2024.100028","url":null,"abstract":"<div><p>Nitro-oxidative stress affects DNA, leading to special chemical modifications of nucleobases and deoxyribose, impacting DNA integrity and stability. Because of the importance of the topic, the state of the knowledge on purine, nucleoside, and DNA nitration by the reactive nitrogen species peroxynitrite was reviewed. Following a description of the chemical and physicochemical characteristics of purines and peroxynitrite, purine nitro-oxidation and its products, the reaction mechanisms, and the recently reported kinetic behavior of 8-NitroGua formation are discussed. Moreover, novel computational studies report structural and conformational DNA changes resulting from the formation of guanine nitration products. Given the relevance of the subject, surprisingly few publications deal with this topic, even considering the past five years.</p></div>","PeriodicalId":101065,"journal":{"name":"Redox Biochemistry and Chemistry","volume":"8 ","pages":"Article 100028"},"PeriodicalIF":0.0,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2773176624000099/pdfft?md5=f15d74688ad9863cfd9c5bb5da57af3b&pid=1-s2.0-S2773176624000099-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141031066","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}