{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,23]],"date-time":"2026-08-23T16:41:55Z","timestamp":1787503315730,"version":"build-2736575974"},"reference-count":109,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2024,9,1]],"date-time":"2024-09-01T00:00:00Z","timestamp":1725148800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,9,1]],"date-time":"2024-09-01T00:00:00Z","timestamp":1725148800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,7,24]],"date-time":"2024-07-24T00:00:00Z","timestamp":1721779200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100010426","name":"UGC-DAE CSR","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100010426","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001502","name":"India Department of Atomic Energy","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001502","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001407","name":"Department of Biotechnology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001407","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001409","name":"Department of Science and Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001409","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100009053","name":"DBT\/Wellcome Trust India Alliance","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100009053","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Redox Biology"],"published-print":{"date-parts":[[2024,9]]},"DOI":"10.1016\/j.redox.2024.103285","type":"journal-article","created":{"date-parts":[[2024,7,31]],"date-time":"2024-07-31T03:12:49Z","timestamp":1722395569000},"page":"103285","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":14,"special_numbering":"C","title":["Intracellular peroxynitrite perturbs redox balance, bioenergetics, and Fe\u2013S cluster homeostasis in Mycobacterium tuberculosis"],"prefix":"10.1016","volume":"75","author":[{"given":"Arshiya","family":"Dewan","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Charu","family":"Jain","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mayashree","family":"Das","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ashutosh","family":"Tripathi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ajay Kumar","family":"Sharma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Harshit","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nitish","family":"Malhotra","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aswin Sai Narain","family":"Seshasayee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Harinath","family":"Chakrapani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6761-1664","authenticated-orcid":false,"given":"Amit","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"4","key":"10.1016\/j.redox.2024.103285_bib1","doi-asserted-by":"crossref","first-page":"1111","DOI":"10.1084\/jem.175.4.1111","article-title":"Killing of virulent Mycobacterium tuberculosis by reactive nitrogen intermediates produced by activated murine macrophages","volume":"175","author":"Chan","year":"1992","journal-title":"J. Exp. Med."},{"issue":"10","key":"10.1016\/j.redox.2024.103285_bib2","doi-asserted-by":"crossref","first-page":"5243","DOI":"10.1073\/pnas.94.10.5243","article-title":"Identification of nitric oxide synthase as a protective locus against tuberculosis","volume":"94","author":"MacMicking","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"4","key":"10.1016\/j.redox.2024.103285_bib3","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1010475","article-title":"Mycobacterium tuberculosis requires SufT for Fe-S cluster maturation, metabolism, and survival in vivo","volume":"18","author":"Tripathi","year":"2022","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.redox.2024.103285_bib4","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2021.102062","article-title":"Mycobacterium tuberculosis SufR responds to nitric oxide via its 4Fe\u20134S cluster and regulates Fe\u2013S cluster biogenesis for persistence in mice","volume":"46","author":"Anand","year":"2021","journal-title":"Redox Biol."},{"issue":"5","key":"10.1016\/j.redox.2024.103285_bib5","doi-asserted-by":"crossref","first-page":"2293","DOI":"10.1084\/jem.183.5.2293","article-title":"Inducible nitric oxide synthase in pulmonary alveolar macrophages from patients with tuberculosis","volume":"183","author":"Nicholson","year":"1996","journal-title":"J. Exp. Med."},{"issue":"9","key":"10.1016\/j.redox.2024.103285_bib6","doi-asserted-by":"crossref","first-page":"3198","DOI":"10.1128\/IAI.00611-13","article-title":"The intracellular environment of human macrophages that produce nitric oxide promotes growth of mycobacteria","volume":"81","author":"Joo-Yong","year":"2013","journal-title":"Infect. Immun."},{"issue":"45","key":"10.1016\/j.redox.2024.103285_bib7","doi-asserted-by":"crossref","first-page":"E4256","DOI":"10.1073\/pnas.1316894110","article-title":"Nitrite produced by Mycobacterium tuberculosis in human macrophages in physiologic oxygen impacts bacterial ATP consumption and gene expression","volume":"110","author":"Cunningham-Bussel","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"2","key":"10.1016\/j.redox.2024.103285_bib8","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1002\/biof.1150","article-title":"Peroxynitrite, a potent macrophage-derived oxidizing cytotoxin to combat invading pathogens","volume":"40","author":"Prolo","year":"2014","journal-title":"Biofactors"},{"issue":"2","key":"10.1016\/j.redox.2024.103285_bib9","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/0165-1110(95)90004-7","article-title":"Potential genotoxicity of chronically elevated nitric oxide: a review","volume":"339","author":"Liu","year":"1995","journal-title":"Mutat. Res. Rev. Genet. Toxicol."},{"issue":"5","key":"10.1016\/j.redox.2024.103285_bib10","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1084\/jem.20030205","article-title":"Inhibition of respiration by nitric oxide induces a Mycobacterium tuberculosis dormancy program","volume":"198","author":"Voskuil","year":"2003","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.redox.2024.103285_bib11","doi-asserted-by":"crossref","DOI":"10.3389\/fmicb.2011.00105","article-title":"The response of Mycobacterium tuberculosis to reactive oxygen and nitrogen species","volume":"2","author":"Voskuil","year":"2011","journal-title":"Front. Microbiol."},{"issue":"2","key":"10.1016\/j.redox.2024.103285_bib12","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1016\/j.bbagen.2013.07.005","article-title":"Kinetic and mechanistic considerations to assess the biological fate of peroxynitrite","volume":"1840","author":"Carballal","year":"2014","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"issue":"2","key":"10.1016\/j.redox.2024.103285_bib13","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1016\/0003-9861(92)90434-X","article-title":"Bactericidal activity of peroxynitrite","volume":"298","author":"Beckman","year":"1992","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.redox.2024.103285_bib14","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1099\/00221287-148-1-307","article-title":"Killing of spores of Bacillus subtilis by peroxynitrite appears to be caused by membrane damage","volume":"N Y","author":"Genest","year":"2002","journal-title":"Microbiology"},{"key":"10.1016\/j.redox.2024.103285_bib15","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1006\/abbi.1995.1044","article-title":"The comparitive toxicity of nitric oxide and peroxynitrite to E.coli","volume":"1","author":"Brunelli","year":"1995","journal-title":"Arch. Biochem. Biophys."},{"issue":"6","key":"10.1016\/j.redox.2024.103285_bib16","doi-asserted-by":"crossref","first-page":"3587","DOI":"10.1128\/IAI.68.6.3587-3593.2000","article-title":"Cooperation between reactive oxygen and nitrogen intermediates in killing of rhodococcus equi by activated macrophages","volume":"68","author":"Darrah","year":"2000","journal-title":"Infect. Immun."},{"issue":"April","key":"10.1016\/j.redox.2024.103285_bib17","first-page":"4953","article-title":"Surfactant protein A mediates mycoplasmacidal activity of alveolar macrophages by production of peroxynitrite","volume":"96","author":"Atalon","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"26","key":"10.1016\/j.redox.2024.103285_bib18","doi-asserted-by":"crossref","first-page":"14243","DOI":"10.1073\/pnas.94.26.14243","article-title":"Peroxynitrite rapidly permeates phospholipid membranes","volume":"94","author":"Marla","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.redox.2024.103285_bib19","series-title":"Diffusion and Transport of Reactive Species across Cell Membranes BT - Bioactive Lipids in Health and Disease","first-page":"3","author":"M\u00f6ller","year":"2019"},{"issue":"1","key":"10.1016\/j.redox.2024.103285_bib20","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/S1074-7613(00)80004-7","article-title":"Phenotype of mice and macrophages deficient in both phagocyte oxidase and inducible nitric oxide synthase","volume":"10","author":"Shiloh","year":"1999","journal-title":"Immunity"},{"issue":"4","key":"10.1016\/j.redox.2024.103285_bib21","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1054\/tuld.1998.0203","article-title":"Toxicity of nitrogen oxides and related oxidants on mycobacteria: M. tuberculosis is resistant to peroxynitrite anion","volume":"79","author":"Yu","year":"1999","journal-title":"Tuber. Lung Dis."},{"issue":"9","key":"10.1016\/j.redox.2024.103285_bib22","doi-asserted-by":"crossref","first-page":"5902","DOI":"10.1073\/pnas.092017799","article-title":"Truncated hemoglobin HbN protects Mycobacterium bovis from nitric oxide","volume":"99","author":"Ouellet","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"9","key":"10.1016\/j.redox.2024.103285_bib23","doi-asserted-by":"crossref","first-page":"3364","DOI":"10.1128\/AAC.00347-07","article-title":"Innate protection of Mycobacterium smegmatis against the antimicrobial activity of nitric oxide is provided by mycothiol","volume":"51","author":"C","year":"2007","journal-title":"Antimicrob. Agents Chemother."},{"issue":"3","key":"10.1016\/j.redox.2024.103285_bib24","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1046\/j.1462-5822.2004.00368.x","article-title":"Production of phthiocerol dimycocerosates protects Mycobacterium tuberculosis from the cidal activity of reactive nitrogen intermediates produced by macrophages and modulates the early immune response to infection","volume":"6","author":"Rousseau","year":"2004","journal-title":"Cell Microbiol."},{"issue":"6801","key":"10.1016\/j.redox.2024.103285_bib25","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1038\/35025109","article-title":"Peroxynitrite reductase activity of bacterial peroxiredoxins","volume":"407","author":"Bryk","year":"2000","journal-title":"Nature"},{"issue":"6","key":"10.1016\/j.redox.2024.103285_bib26","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1005675","article-title":"Mycobacterium tuberculosis thioredoxin reductase is essential for thiol redox homeostasis but plays a minor role in antioxidant defense","volume":"12","author":"Lin","year":"2016","journal-title":"PLoS Pathog."},{"issue":"5","key":"10.1016\/j.redox.2024.103285_bib27","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.micpath.2006.01.004","article-title":"Truncated hemoglobin GlbO from Mycobacterium leprae alleviates nitric oxide toxicity","volume":"40","author":"Fabozzi","year":"2006","journal-title":"Microb. Pathog."},{"issue":"3","key":"10.1016\/j.redox.2024.103285_bib28","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1006\/bbrc.1999.0358","article-title":"Mycobacterium tuberculosisKatG is a peroxynitritase","volume":"256","author":"Wengenack","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"5906","key":"10.1016\/j.redox.2024.103285_bib29","doi-asserted-by":"crossref","first-page":"1392","DOI":"10.1126\/science.1164571","article-title":"PA-824 kills nonreplicating Mycobacterium tuberculosis by intracellular NO release","volume":"322","author":"Singh","year":"1979","journal-title":"Science"},{"key":"10.1016\/j.redox.2024.103285_bib30","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1016\/j.freeradbiomed.2015.03.008","article-title":"Mycobacterium tuberculosis has diminished capacity to counteract redox stress induced by elevated levels of endogenous superoxide","volume":"84","author":"Tyagi","year":"2015","journal-title":"Free Radic. Biol. Med."},{"issue":"7","key":"10.1016\/j.redox.2024.103285_bib31","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1084\/jem.20021186","article-title":"\u201c virulent but not avirulent Mycobacterium tuberculosis can evade the growth inhibitory action of a T helper 1\u2013dependent, nitric oxide synthase 2\u2013independent defense in mice \u201d","volume":"196","author":"Jung","year":"2002","journal-title":"J. Exp. Med."},{"issue":"7","key":"10.1016\/j.redox.2024.103285_bib32","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.pone.0181221","article-title":"Reduced susceptibility of clinical strains of Mycobacterium tuberculosis to reactive nitrogen species promotes survival in activated macrophages","volume":"12","author":"Idh","year":"2017","journal-title":"PLoS One"},{"issue":"3","key":"10.1016\/j.redox.2024.103285_bib33","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1021\/cb800279q","article-title":"Chemical biology of peroxynitrite: kinetics, diffusion, and radicals","volume":"4","author":"Ferrer-Sueta","year":"2009","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.redox.2024.103285_bib34","series-title":"Peroxynitrite Detection in Biological Media","author":"Peteu","year":"2015"},{"issue":"5","key":"10.1016\/j.redox.2024.103285_bib35","doi-asserted-by":"crossref","DOI":"10.3390\/cells12050682","article-title":"A beginner's guide to cell culture: practical advice for preventing needless problems","volume":"12","author":"Weiskirchen","year":"2023","journal-title":"Cells"},{"issue":"6","key":"10.1016\/j.redox.2024.103285_bib36","doi-asserted-by":"crossref","first-page":"1274","DOI":"10.1021\/acs.orglett.6b00186","article-title":"A small molecule for controlled generation of peroxynitrite","volume":"18","author":"Khodade","year":"2016","journal-title":"Org. Lett."},{"issue":"9","key":"10.1016\/j.redox.2024.103285_bib37","article-title":"Moxifloxacin-mediated killing of Mycobacterium tuberculosis involves respiratory downshift, reductive stress, and accumulation of reactive oxygen species","volume":"66","author":"Somnath","year":"2022","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.redox.2024.103285_bib38","article-title":"Cysteine desulfurase (IscS)-mediated fine-tuning of bioenergetics and SUF expression prevents Mycobacterium tuberculosis hypervirulence (in press)","volume":"9","author":"Mayashree Das","year":"2023","journal-title":"Sci. Adv."},{"issue":"9","key":"10.1016\/j.redox.2024.103285_bib39","doi-asserted-by":"crossref","first-page":"1793","DOI":"10.1021\/tx300164j","article-title":"Boronate probes as diagnostic tools for real time monitoring of peroxynitrite and hydroperoxides","volume":"25","author":"Jacek Zielonka","year":"2012","journal-title":"Chem. Res. Toxicol."},{"issue":"10","key":"10.1016\/j.redox.2024.103285_bib40","doi-asserted-by":"crossref","first-page":"1401","DOI":"10.1016\/j.freeradbiomed.2009.08.006","article-title":"Free Radical Biology & Medicine Direct oxidation of boronates by peroxynitrite : mechanism and implications in fl uorescence imaging of peroxynitrite","volume":"47","author":"Sikora","year":"2009","journal-title":"Free Radic. Biol. Med."},{"issue":"2","key":"10.1016\/j.redox.2024.103285_bib41","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.ab.2005.11.003","article-title":"Synthesis of peroxynitrite using isoamyl nitrite and hydrogen peroxide in a homogeneous solvent system","volume":"354","author":"Uppu","year":"2006","journal-title":"Anal. Biochem."},{"issue":"1","key":"10.1016\/j.redox.2024.103285_bib42","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1003902","article-title":"Reengineering redox sensitive GFP to measure mycothiol redox potential of Mycobacterium tuberculosis during infection","volume":"10","author":"Bhaskar","year":"2014","journal-title":"PLoS Pathog."},{"issue":"1","key":"10.1016\/j.redox.2024.103285_bib43","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1003902","article-title":"Reengineering redox sensitive GFP to measure mycothiol redox potential of Mycobacterium tuberculosis during infection","volume":"10","author":"Bhaskar","year":"2014","journal-title":"PLoS Pathog."},{"issue":"November","key":"10.1016\/j.redox.2024.103285_bib44","article-title":"Targeting redox heterogeneity to counteract drug tolerance in replicating Mycobacterium tuberculosis","volume":"6635","author":"Mishra","year":"2019","journal-title":"Sci. Transl. Med."},{"issue":"14","key":"10.1016\/j.redox.2024.103285_bib45","doi-asserted-by":"crossref","first-page":"1754","DOI":"10.1093\/bioinformatics\/btp324","article-title":"Fast and accurate short read alignment with Burrows \u2013 wheeler transform","volume":"25","author":"Li","year":"2009","journal-title":"Bioinformatics"},{"issue":"16","key":"10.1016\/j.redox.2024.103285_bib46","doi-asserted-by":"crossref","first-page":"2078","DOI":"10.1093\/bioinformatics\/btp352","article-title":"The sequence alignment\/map format and SAMtools","volume":"25","author":"Li","year":"2009","journal-title":"Bioinformatics"},{"issue":"6","key":"10.1016\/j.redox.2024.103285_bib47","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1093\/bioinformatics\/btq033","article-title":"BEDTools : a flexible suite of utilities for comparing genomic features","volume":"26","author":"Quinlan","year":"2010","journal-title":"Bioinformatics"},{"issue":"1","key":"10.1016\/j.redox.2024.103285_bib48","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1093\/bioinformatics\/btp616","article-title":"edgeR : a Bioconductor package for differential expression analysis of digital gene expression data","volume":"26","author":"Robinson","year":"2010","journal-title":"Bioinformatics"},{"key":"10.1016\/j.redox.2024.103285_bib49","first-page":"1","article-title":"From reads to genes to pathways : differential expression analysis of RNA-Seq experiments using Rsubread and the edgeR quasi-likelihood pipeline [ version 2 ; referees : 5 approved ] Referee Status","author":"Chen","year":"2016","journal-title":"F1000Res"},{"issue":"25","key":"10.1016\/j.redox.2024.103285_bib50","doi-asserted-by":"crossref","first-page":"eabo0097","DOI":"10.1126\/sciadv.abo0097","article-title":"S-Adenosylmethionine\u2013responsive cystathionine \u03b2-synthase modulates sulfur metabolism and redox balance in Mycobacterium tuberculosis","volume":"8","author":"Bandyopadhyay","year":"2022","journal-title":"Sci. Adv."},{"key":"10.1016\/j.redox.2024.103285_bib51","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms12393","article-title":"Turning the respiratory flexibility of Mycobacterium tuberculosis against itself","author":"Lamprecht","year":"2016","journal-title":"Nat. Commun."},{"issue":"April","key":"10.1016\/j.redox.2024.103285_bib52","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.niox.2020.04.005","article-title":"Isolation and culture of murine bone marrow-derived macrophages for nitric oxide and redox biology","volume":"100\u2013101","author":"Bailey","year":"2020","journal-title":"Nitric Oxide"},{"issue":"10","key":"10.1016\/j.redox.2024.103285_bib53","doi-asserted-by":"crossref","first-page":"1401","DOI":"10.1016\/j.freeradbiomed.2009.08.006","article-title":"Direct oxidation of boronates by peroxynitrite: mechanism and implications in fluorescence imaging of peroxynitrite","volume":"47","author":"Sikora","year":"2009","journal-title":"Free Radic. Biol. Med."},{"issue":"10","key":"10.1016\/j.redox.2024.103285_bib54","doi-asserted-by":"crossref","first-page":"2610","DOI":"10.1021\/ol5010643","article-title":"Arylboronate ester based diazeniumdiolates (BORO\/NO), a class of hydrogen peroxide inducible nitric oxide (NO) donors","volume":"16","author":"Dharmaraja","year":"2014","journal-title":"Org. Lett."},{"key":"10.1016\/j.redox.2024.103285_bib55","unstructured":"K. Lin, S. Wu, K. Hsu, C. Hung, W. Liaw, and Y. Wang, \u201cA Ds-DAB Based Fluorescent Chemosensor for Peroxynitrite,\u201d pp. 1\u201313."},{"issue":"8","key":"10.1016\/j.redox.2024.103285_bib56","doi-asserted-by":"crossref","first-page":"5228","DOI":"10.1074\/jbc.M113.510248","article-title":"Mycothiol\/mycoredoxin 1-dependent reduction of the peroxiredoxin AhpE from Mycobacterium tuberculosis","volume":"289","author":"Hugo","year":"2014","journal-title":"J. Biol. Chem."},{"issue":"11","key":"10.1016\/j.redox.2024.103285_bib57","doi-asserted-by":"crossref","first-page":"3616","DOI":"10.1128\/AAC.47.11.3616-3619.2003","article-title":"Resazurin microtiter assay plate testing of Mycobacterium tuberculosis susceptibilities to second-line drugs: rapid, simple, and inexpensive method","volume":"47","author":"Anandi","year":"2003","journal-title":"Antimicrob. Agents Chemother."},{"issue":"8","key":"10.1016\/j.redox.2024.103285_bib58","doi-asserted-by":"crossref","first-page":"2720","DOI":"10.1128\/AAC.46.8.2720-2722.2002","article-title":"Resazurin microtiter assay plate: simple and inexpensive method for detection of drug resistance in Mycobacterium tuberculosis","volume":"46","author":"Juan-Carlos","year":"2002","journal-title":"Antimicrob. Agents Chemother."},{"issue":"3","key":"10.1016\/j.redox.2024.103285_bib59","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1006\/bbrc.1999.0358","article-title":"Mycobacterium tuberculosis KatG is a peroxynitritase","volume":"256","author":"Wengenack","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"5557","key":"10.1016\/j.redox.2024.103285_bib60","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1126\/science.1067798","article-title":"Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein","volume":"295","author":"Bryk","year":"1979","journal-title":"Science"},{"key":"10.1016\/j.redox.2024.103285_bib61","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1046\/j.1365-2958.2002.03005.x","article-title":"Role of the extracytoplasmic-function sigma Factor SigH in Mycobacterium tuberculosis global gene expression","volume":"45","author":"Manganelli","year":"2002","journal-title":"Mol. Microbiol."},{"issue":"20","key":"10.1016\/j.redox.2024.103285_bib62","doi-asserted-by":"crossref","first-page":"6119","DOI":"10.1128\/JB.183.20.6119-6125.2001","article-title":"The alternative sigma factor SigH regulates major components of oxidative and heat stress responses in Mycobacterium tuberculosis","volume":"183","author":"Raman","year":"2001","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.redox.2024.103285_bib63","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.freeradbiomed.2018.11.032","article-title":"Mycobacterium tuberculosis WhiB3 maintains redox homeostasis and survival in response to reactive oxygen and nitrogen species","author":"Mehta","year":"2019","journal-title":"Free Radic. Biol. Med."},{"issue":"7","key":"10.1016\/j.redox.2024.103285_bib64","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0200145","article-title":"Rv1460, a SufR homologue, is a repressor of the suf operon in Mycobacterium tuberculosis","volume":"13","author":"Willemse","year":"2018","journal-title":"PLoS One"},{"issue":"44","key":"10.1016\/j.redox.2024.103285_bib65","doi-asserted-by":"crossref","first-page":"27652","DOI":"10.1074\/jbc.272.44.27652","article-title":"Inactivation of dehydratase [4Fe-4S] clusters and disruption of iron homeostasis upon cell exposure to peroxynitrite","volume":"272","author":"Keyer","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.redox.2024.103285_bib66","first-page":"12","article-title":"Bacterial cysteine desulfurases : their function and mechanisms","author":"Mihara","year":"2002","journal-title":"Appl. Microbiol. Biotechnol."},{"issue":"7","key":"10.1016\/j.redox.2024.103285_bib67","doi-asserted-by":"crossref","DOI":"10.3390\/antiox10070997","article-title":"The multifaceted bacterial cysteine desulfurases: from metabolism to pathogenesis","volume":"10","author":"Das","year":"2021","journal-title":"Antioxidants"},{"issue":"10","key":"10.1016\/j.redox.2024.103285_bib68","doi-asserted-by":"crossref","DOI":"10.3390\/inorganics10100174","article-title":"Iron-sulfur clusters toward stresses: implication for understanding and fighting tuberculosis","volume":"10","author":"Elchennawi","year":"2022","journal-title":"INORGA"},{"issue":"4","key":"10.1016\/j.redox.2024.103285_bib69","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1007\/s00775-017-1527-3","article-title":"Iron\u2013sulfur clusters biogenesis by the SUF machinery: close to the molecular mechanism understanding","volume":"23","author":"P\u00e9rard","year":"2018","journal-title":"JBIC, J. Biol. Inorg. Chem."},{"issue":"37","key":"10.1016\/j.redox.2024.103285_bib70","doi-asserted-by":"crossref","first-page":"26464","DOI":"10.1074\/jbc.R113.472936","article-title":"Peroxynitrite, a stealthy biological oxidant","volume":"288","author":"Radi","year":"2013","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.redox.2024.103285_bib71","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1002\/biof.1150","article-title":"Peroxynitrite, a potent macrophage-derived oxidizing cytotoxin to Combat Invading Pathogens","volume":"40","author":"Prolo","year":"2015","journal-title":"Biofactors"},{"issue":"7","key":"10.1016\/j.redox.2024.103285_bib72","doi-asserted-by":"crossref","first-page":"4244","DOI":"10.1016\/S0021-9258(20)64313-7","article-title":"Peroxynitrite oxidation of sulfhydryls","volume":"266","author":"Radil","year":"1991","journal-title":"J. Biol. Chem."},{"issue":"23","key":"10.1016\/j.redox.2024.103285_bib73","doi-asserted-by":"crossref","first-page":"5839","DOI":"10.1073\/pnas.1804932115","article-title":"Oxygen radicals, nitric oxide, and peroxynitrite: redox pathways in molecular medicine","volume":"115","author":"Radi","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.redox.2024.103285_bib74","doi-asserted-by":"crossref","DOI":"10.3389\/fcimb.2022.876667","article-title":"The iron response of Mycobacterium tuberculosis and its implications for tuberculosis pathogenesis and novel therapeutics","volume":"12","author":"Rodriguez","year":"2022","journal-title":"Front. Cell. Infect. Microbiol."},{"issue":"7","key":"10.1016\/j.redox.2024.103285_bib75","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1016\/j.tim.2006.05.006","article-title":"Control of iron metabolism in Mycobacterium tuberculosis","volume":"14","author":"Rodriguez","year":"2006","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.redox.2024.103285_bib76","doi-asserted-by":"crossref","first-page":"618","DOI":"10.1016\/j.redox.2017.09.009","article-title":"Fundamentals on the biochemistry of peroxynitrite and protein tyrosine nitration","volume":"14","author":"Bartesaghi","year":"2018","journal-title":"Redox Biol."},{"issue":"1","key":"10.1016\/j.redox.2024.103285_bib77","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/0014-5793(94)80582-2","article-title":"Peroxynitrite releases copper from caeruloplasmin: implications for atherosclerosis","volume":"342","author":"Swain","year":"1994","journal-title":"FEBS Lett."},{"issue":"2","key":"10.1016\/j.redox.2024.103285_bib78","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1002\/mnfr.200600107","article-title":"Impact of copper on the induction and repair of oxidative DNA damage, poly(ADP-ribosyl)ation and PARP-1 activity","volume":"51","author":"Schwerdtle","year":"2007","journal-title":"Mol. Nutr. Food Res."},{"issue":"1","key":"10.1016\/j.redox.2024.103285_bib79","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.mrfmmm.2012.03.010","article-title":"The relationship of copper to DNA damage and damage prevention in humans","volume":"733","author":"Linder","year":"2012","journal-title":"Mutat. Res., Fundam. Mol. Mech. Mutagen."},{"issue":"6","key":"10.1016\/j.redox.2024.103285_bib80","doi-asserted-by":"crossref","first-page":"929","DOI":"10.1039\/C4MT00305E","article-title":"Copper homeostasis in Mycobacterium tuberculosis","volume":"7","author":"Shi","year":"2015","journal-title":"Metallomics"},{"issue":"October 2010","key":"10.1016\/j.redox.2024.103285_bib81","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1111\/j.1365-2958.2010.07431.x","article-title":"A novel copper-responsive regulon in Mycobacterium tuberculosis","volume":"79","author":"Festa","year":"2011","journal-title":"Mol. Microbiol."},{"issue":"2","key":"10.1016\/j.redox.2024.103285_bib82","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/0003-9861(91)90224-7","article-title":"Peroxynitrite-induced membrane lipid peroxidation: the cytotoxic potential of superoxide and nitric oxide","volume":"288","author":"Radi","year":"1991","journal-title":"Arch. Biochem. Biophys."},{"issue":"1","key":"10.1016\/j.redox.2024.103285_bib83","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1128\/CMR.18.1.81-101.2005","article-title":"Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis","volume":"18","author":"Kuni","year":"2005","journal-title":"Clin. Microbiol. Rev."},{"issue":"47","key":"10.1016\/j.redox.2024.103285_bib84","doi-asserted-by":"crossref","first-page":"29409","DOI":"10.1016\/S0021-9258(18)43894-X","article-title":"Aconitase is readily inactivated by peroxynitrite, but not by its precursor, nitric oxide","volume":"269","author":"Castro","year":"1994","journal-title":"J. Biol. Chem."},{"issue":"40","key":"10.1016\/j.redox.2024.103285_bib85","doi-asserted-by":"crossref","first-page":"25071","DOI":"10.1074\/jbc.272.40.25071","article-title":"Nitric oxide sensitivity of the aconitases","volume":"272","author":"Gardner","year":"1997","journal-title":"J. Biol. Chem."},{"issue":"11","key":"10.1016\/j.redox.2024.103285_bib86","doi-asserted-by":"crossref","first-page":"4046","DOI":"10.1128\/JB.00026-07","article-title":"Iron-dependent RNA-binding activity of Mycobacterium tuberculosis aconitase","volume":"189","author":"Banerjee","year":"2007","journal-title":"J. Bacteriol."},{"issue":"3","key":"10.1016\/j.redox.2024.103285_bib87","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1042\/BJ20130732","article-title":"The cysteine desulfurase IscS of Mycobacterium tuberculosis is involved in iron-sulfur cluster biogenesis and oxidative stress defence","volume":"459","author":"Rybniker","year":"2014","journal-title":"Biochem. J."},{"issue":"1\u20132","key":"10.1016\/j.redox.2024.103285_bib88","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.cbpa.2012.03.004","article-title":"Iron sulfur cluster proteins and microbial regulation: implications for understanding tuberculosis","volume":"16","author":"Saini","year":"2012","journal-title":"Curr. Opin. Chem. Biol."},{"issue":"16","key":"10.1016\/j.redox.2024.103285_bib89","doi-asserted-by":"crossref","first-page":"8841","DOI":"10.1073\/pnas.97.16.8841","article-title":"Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens","volume":"97","author":"Nathan","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"3","key":"10.1016\/j.redox.2024.103285_bib90","doi-asserted-by":"crossref","first-page":"215","DOI":"10.4161\/cib.2.3.7926","article-title":"The mechanism of action of PA-824","volume":"2","author":"Manjunatha","year":"2009","journal-title":"Commun. Integr. Biol."},{"key":"10.1016\/j.redox.2024.103285_bib91","doi-asserted-by":"crossref","first-page":"2815","DOI":"10.2147\/DDDT.S281639","article-title":"Profiling pretomanid as a therapeutic option for TB infection: evidence to date","volume":"15","author":"Stancil","year":"2021","journal-title":"Drug Des. Dev. Ther."},{"key":"10.1016\/j.redox.2024.103285_bib92","doi-asserted-by":"crossref","DOI":"10.3389\/fphar.2023.1100488","article-title":"Clofazimine for the treatment of tuberculosis","volume":"14","author":"Stadler","year":"2023","journal-title":"Front. Pharmacol."},{"issue":"5","key":"10.1016\/j.redox.2024.103285_bib93","article-title":"The promises and limitations of N-acetylcysteine as a potentiator of first-line and second-line tuberculosis drugs","volume":"65","author":"Catherine","year":"2021","journal-title":"Antimicrob. Agents Chemother."},{"issue":"3","key":"10.1016\/j.redox.2024.103285_bib94","article-title":"Vitamin C potentiates the killing of Mycobacterium tuberculosis by the first-line tuberculosis drugs isoniazid and rifampin in mice","volume":"62","author":"Catherine","year":"2018","journal-title":"Antimicrob. Agents Chemother."},{"issue":"1","key":"10.1016\/j.redox.2024.103285_bib95","doi-asserted-by":"crossref","first-page":"1881","DOI":"10.1038\/ncomms2898","article-title":"Mycobacterium tuberculosis is extraordinarily sensitive to killing by a vitamin C-induced Fenton reaction","volume":"4","author":"Vilch\u00e8ze","year":"2013","journal-title":"Nat. Commun."},{"key":"10.1016\/j.redox.2024.103285_bib96","doi-asserted-by":"crossref","first-page":"815","DOI":"10.2147\/IDR.S240716","article-title":"Comparison of in vitro susceptibility of mycobacteria against PA-824 to identify key residues of ddn, the deazoflavin-dependent nitroreductase from Mycobacterium tuberculosis","volume":"13","author":"Zhang","year":"2020","journal-title":"Infect. Drug Resist."},{"issue":"11","key":"10.1016\/j.redox.2024.103285_bib97","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0111680","article-title":"Regulation of the ahpC gene encoding alkyl hydroperoxide reductase in Mycobacterium smegmatis","volume":"9","author":"Lee","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.redox.2024.103285_bib98","doi-asserted-by":"crossref","DOI":"10.1016\/j.gene.2022.146759","article-title":"Transcript analysis and expression of the glbO gene, encoding truncated hemoglobin,O, of M. Smegmatis implicate its role under hypoxia and oxidative stress","volume":"841","author":"Chhaya","year":"2022","journal-title":"Gene"},{"issue":"7","key":"10.1016\/j.redox.2024.103285_bib99","doi-asserted-by":"crossref","first-page":"4281","DOI":"10.1074\/jbc.274.7.4281","article-title":"Export of recombinant Mycobacterium tuberculos is superoxide dismutase is dependent upon both information in the protein and mycobacterial export machinery: a model for studying export of leaderless proteins by pathogenic mycobacteria","volume":"274","author":"Harth","year":"1999","journal-title":"J. Biol. Chem."},{"issue":"January","key":"10.1016\/j.redox.2024.103285_bib100","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1111\/j.1365-2958.2006.05028.x","article-title":"Iron-sulphur clusters and the problem with oxygen","volume":"59","author":"Imlay","year":"2006","journal-title":"Mol. Microbiol."},{"issue":"2","key":"10.1016\/j.redox.2024.103285_bib101","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1006\/abbi.1996.0178","article-title":"Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport","volume":"328","author":"Cassina","year":"1996","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.redox.2024.103285_bib102","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.bbabio.2004.03.016","article-title":"Inhibition of mitochondrial respiratory complex I by nitric oxide , peroxynitrite and S-nitrosothiols","volume":"1658","author":"Brown","year":"2004","journal-title":"Biochim. Biophys. Acta, Bioenerg."},{"key":"10.1016\/j.redox.2024.103285_bib103","first-page":"139","article-title":"Nitric oxide inhibits mitochondrial NADH:ubiquinone reductase activity through peroxynitrite formation","volume":"145","author":"Clementi","year":"2001","journal-title":"Biochem. J."},{"issue":"2","key":"10.1016\/j.redox.2024.103285_bib104","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1006\/abbi.1995.1321","article-title":"Kinetics of cytochrome c2+ oxidation by peroxynitrite: implications for superoxide measurements in nitric oxide-producing biological systems","volume":"319","author":"Thomson","year":"1995","journal-title":"Arch. Biochem. Biophys."},{"issue":"February","key":"10.1016\/j.redox.2024.103285_bib105","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1016\/0006-2952(96)99426-5","article-title":"Alterations to glutathione and nicotinamide nucleotides during the mitochondrial permeability transition induced by peroxynitrite","volume":"52","author":"Scarlett","year":"1996","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.redox.2024.103285_bib106","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1080\/10715760100300451","article-title":"Peroxynitrite promotes mitochondrial permeability transition-dependent rapid U937 cell necrosis : survivors proliferate with kinetics superimposable on those of untreated cells","author":"Sestili","year":"2001","journal-title":"Free Radic. Res."},{"issue":"1","key":"10.1016\/j.redox.2024.103285_bib107","doi-asserted-by":"crossref","first-page":"37","DOI":"10.3109\/10715762.2010.516254","article-title":"Mitochondrial protein tyrosine nitration","volume":"45","author":"Castro","year":"2011","journal-title":"Free Radic. Res."},{"issue":"1","key":"10.1016\/j.redox.2024.103285_bib108","doi-asserted-by":"crossref","first-page":"C80","DOI":"10.1152\/ajpcell.00073.2015","article-title":"Nitrotyrosine impairs mitochondrial function in fetal lamb pulmonary artery endothelial cells","volume":"310","author":"Teng","year":"2015","journal-title":"Am. J. Physiol. Cell Physiol."},{"issue":"22","key":"10.1016\/j.redox.2024.103285_bib109","doi-asserted-by":"crossref","first-page":"8530","DOI":"10.1074\/jbc.RA117.000883","article-title":"The labile iron pool attenuates peroxynitrite-dependent damage and can no longer be considered solely a pro-oxidative cellular iron source","volume":"293","author":"Damasceno","year":"2018","journal-title":"J. Biol. Chem."}],"container-title":["Redox Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2213231724002635?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2213231724002635?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,10,10]],"date-time":"2024-10-10T01:11:48Z","timestamp":1728522708000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2213231724002635"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,9]]},"references-count":109,"alternative-id":["S2213231724002635"],"URL":"https:\/\/doi.org\/10.1016\/j.redox.2024.103285","relation":{},"ISSN":["2213-2317"],"issn-type":[{"value":"2213-2317","type":"print"}],"subject":[],"published":{"date-parts":[[2024,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Intracellular peroxynitrite perturbs redox balance, bioenergetics, and Fe\u2013S cluster homeostasis in Mycobacterium tuberculosis","name":"articletitle","label":"Article Title"},{"value":"Redox Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.redox.2024.103285","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"103285"}}