{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,4]],"date-time":"2026-06-04T14:23:39Z","timestamp":1780583019075,"version":"3.54.1"},"reference-count":67,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2025,3,11]],"date-time":"2025-03-11T00:00:00Z","timestamp":1741651200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004504","name":"Lithuanian-French collaboration program Gilibert","doi-asserted-by":"publisher","award":["S-LZ-23-2"],"award-info":[{"award-number":["S-LZ-23-2"]}],"id":[{"id":"10.13039\/501100004504","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004504","name":"Lithuanian-French collaboration program Gilibert","doi-asserted-by":"publisher","award":["48890RJ"],"award-info":[{"award-number":["48890RJ"]}],"id":[{"id":"10.13039\/501100004504","id-type":"DOI","asserted-by":"publisher"}]},{"name":"COST action CA21111","award":["S-LZ-23-2"],"award-info":[{"award-number":["S-LZ-23-2"]}]},{"name":"COST action CA21111","award":["48890RJ"],"award-info":[{"award-number":["48890RJ"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>In order to detail the antiplasmodial effects of quinones (Q) and nitroaromatic compounds (ArNO2), we investigated their reduction mechanism by Plasmodium falciparum flavoenzyme type II NADH:ubiquinone oxidoreductase (PfNDH2). The reactivity of Q and ArNO2 (n = 29) follows a common trend and exhibits a parabolic dependence on their single-electron reduction potential (E71), albeit with significantly scattered data. The reactivity of quinones with similar E71 values increases with their lipophilicity. Quinones are reduced by PfNDH2 in a two-electron way, but ArNO2 are reduced in a single-electron way. The inhibition studies using NAD+ and ADP-ribose showed that quinones oxidize the complexes of reduced enzyme with NADH and NAD+. This suggests that, as in the case of other NDH2s, quinones and the nicotinamide ring of NAD(H) bind at separate sites. A scheme of PfNDH2 catalysis is proposed, consistent with both the observed \u2018ping-pong\u2019 mechanism and the presence of two substrate binding sites. Molecular docking showed that Q and ArNO2 bind in a similar manner and that lipophilic quinones have a higher affinity for the binding site. One may expect that PfNDH2 can be partially responsible for the previously observed enhanced antiplasmodial activity of aziridinylbenzoquinones caused by their two-electron reduction, as well as for the redox cycling and oxidative stress-type action of ArNO2.<\/jats:p>","DOI":"10.3390\/ijms26062509","type":"journal-article","created":{"date-parts":[[2025,3,11]],"date-time":"2025-03-11T08:59:52Z","timestamp":1741683592000},"page":"2509","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Reactions of Plasmodium falciparum Type II NADH: Ubiquinone Oxidoreductase with Nonphysiological Quinoidal and Nitroaromatic Oxidants"],"prefix":"10.3390","volume":"26","author":[{"given":"Lina","family":"Misevi\u010dien\u0117","sequence":"first","affiliation":[{"name":"Department of Xenobiotics Biochemistry, Institute of Biochemistry of Vilnius University, Saul\u0117tekio 7, LT-10257 Vilnius, Lithuania"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6738-8631","authenticated-orcid":false,"given":"Marie-Pierre","family":"Golinelli-Cohen","sequence":"additional","affiliation":[{"name":"Institut de Chimie des Substances Naturelles, UPR2301, CNRS, Universit\u00e9 Paris-Saclay, 1, Avenue de la Terrasse, 99198 Gif-sur-Yvette, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5427-0175","authenticated-orcid":false,"given":"Visvaldas","family":"Kairys","sequence":"additional","affiliation":[{"name":"Department of Bioinformatics, Institute of Biotechnology of Vilnius University, Saul\u0117tekio 7, LT-10257 Vilnius, Lithuania"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Audron\u0117","family":"Marozien\u0117","sequence":"additional","affiliation":[{"name":"Department of Xenobiotics Biochemistry, Institute of Biochemistry of Vilnius University, Saul\u0117tekio 7, LT-10257 Vilnius, Lithuania"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3069-5734","authenticated-orcid":false,"given":"Mindaugas","family":"Lesanavi\u010dius","sequence":"additional","affiliation":[{"name":"Department of Xenobiotics Biochemistry, Institute of Biochemistry of Vilnius University, Saul\u0117tekio 7, LT-10257 Vilnius, Lithuania"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Narimantas","family":"\u010c\u0117nas","sequence":"additional","affiliation":[{"name":"Department of Xenobiotics Biochemistry, Institute of Biochemistry of Vilnius University, Saul\u0117tekio 7, LT-10257 Vilnius, Lithuania"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,3,11]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1038\/nature15535","article-title":"The effect of malaria control on Plasmodium falciparum in Africa between 2000 and 2015","volume":"526","author":"Bhatt","year":"2015","journal-title":"Nature"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1038\/nrmicro.2017.161","article-title":"Drug resistance in Plasmodium","volume":"16","author":"Haldar","year":"2018","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Pal, C. (2023). Redox modulating small molecules having antimalarial activity. Biochem. Pharmacol., 218.","DOI":"10.1016\/j.bcp.2023.115927"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1634","DOI":"10.1021\/jm00109a016","article-title":"Synthesis and antimalarial activity of 2-aziridinyl- and 2,3-bis(aziridinyl)-1,4-naphthoquinone sulfonate and acylate derivatives","volume":"34","author":"Lin","year":"1991","journal-title":"J. Med. Chem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.abb.2009.11.012","article-title":"Antiplasmodial activity of quinones: Roles of aziridinyl substituents and inhibition of Plasmodium falciparum glutathione reductase","volume":"494","author":"Grellier","year":"2010","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Marozien\u0117, A., Lesanavi\u010dius, M., Davioud-Charvet, E., Aliverti, A., Grellier, P., \u0160arlauskas, J., and \u010c\u0117nas, N. (2019). Antiplasmodial activity of nitroaromatic compounds: Correlation with their reduction potential and inhibitory activity on Plasmodium falciparum glutathione reductase. Molecules, 24.","DOI":"10.3390\/molecules24244509"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"e0268320","DOI":"10.1128\/AAC.02683-20","article-title":"Antimicrobial activities of (Z)-2-(nitroheteroarylmethylene)-3-(2H)-benzofuranone derivatives: In vitro and in vivo assessment and \u03b2-hematin formation ihibition activity","volume":"65","author":"Navidpour","year":"2021","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.ijpddr.2022.05.004","article-title":"3-Nitroimidazo{1,2-b]pyridazine as a novel scaffold for antiparasitics with sub-nanomolar anti-Giardia liamblia activity","volume":"19","author":"Zheng","year":"2022","journal-title":"Int. J. Parasitol. Drugs Drug Resist."},{"key":"ref_9","doi-asserted-by":"crossref","unstructured":"Shafi, S., Gupta, S., Jain, R., Shoaib, R., Munjal, A., Maurya, P., Kumar, P., Najmi, K., and Singh, S. (2023). Tackling the emerging artemsiin-resistant malaria parasite by modulation of defensive oxido-reductase mechanism via nitrofurantoin repurposing. Biochem. Pharmacol., 215.","DOI":"10.1016\/j.bcp.2023.115756"},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Lopez-Mercado, S., Enriquez, C., Valderrama, J.A., Pino-Rios, R., Ruis-Vasquea, L., Ruiz Mesia, L., Vargas-Arana, G., Buc Calderon, P., and Benitez, J. (2024). Exploring the antibacterial and antiparasitic activity of phenylaminonaphthoquinones\u2013green synthesis, biologivcal evaluations and computational studies. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms251910670"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1038\/nature05572","article-title":"Specific role of mitochondrial electron transport in blood-stage Plasmodium falciparum","volume":"446","author":"Painter","year":"2007","journal-title":"Nature"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"8298","DOI":"10.1073\/pnas.1205651109","article-title":"Generation of quinolone antimalarials targeting the Plasmodium falciparum mitochondrial respiratory chain for the treatment and prophylaxis of malaria","volume":"109","author":"Biagini","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1831","DOI":"10.1021\/jm201179h","article-title":"Identification, design and biological evaluation of bisaryl quinolones targeting Plasmodium falciparum type II NADH:quinone oxidoreductase (PfNDH2)","volume":"55","author":"Pidathala","year":"2012","journal-title":"J. Med. Chem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1994","DOI":"10.1021\/acs.jmedchem.6b01733","article-title":"Target elucidation by cocrystal structures of NADH-ubiquinone oxidoreductase of Plasmodium falciparum with small molecule to eliminate drug-resistant malaria","volume":"60","author":"Yang","year":"2017","journal-title":"J. Med. Chem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1006\/abbi.2001.2293","article-title":"Kinetic characterization of the rotenone-insensitive internal NADH:ubiquinone oxidoreductase of mitochondria of Saccharomyces cerevisiae","volume":"389","author":"Velazquez","year":"2001","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"6012","DOI":"10.1074\/jbc.M610646200","article-title":"Roles of bound quinone in the single subunit NADH-quinone oxidoreductase (Ndi1) from Saccharomyces cerevisiae","volume":"282","author":"Yamashita","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"9287","DOI":"10.1074\/jbc.M110.175547","article-title":"Reaction mechanism of single subunit NADH-ubiquinone oxidoreductase (Ndi1) from Saccharomyces cerevisiae. Evidence for a ternary complex mechanism","volume":"286","author":"Yang","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"478","DOI":"10.1038\/nature11541","article-title":"Structural insights into the type-II mitochondrial NADH dehydrogenases","volume":"491","author":"Feng","year":"2012","journal-title":"Nature"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.1021\/bi4013897","article-title":"Mycobacterium tuberculosis type II NADH-menaquinone oxidoreductase catalyzes electron transfer through a two-site ping-pong mechanism and has two quinone-binding sites","volume":"53","author":"Yano","year":"2014","journal-title":"Biochemistry"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"950","DOI":"10.1111\/mmi.12507","article-title":"Structure of the bacterial type II NADH dehydrogenase: A monotopic membrane protein with an essential role in energy generation","volume":"91","author":"Heikal","year":"2014","journal-title":"Mol. Microbiol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1111\/mmi.13120","article-title":"Type-II NADH:quinone oxidoreductase from Staphylococcus aureus has two distinct binding sites and is rate limited by quinone reduction","volume":"98","author":"Sena","year":"2015","journal-title":"Mol. Microbiol."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Blaza, J.N., Bridges, H.R., Aragao, D., Dunn, E.A., Heikal, A., Cook, G.M., Nakatani, Y., and Hirst, J. (2017). The mechanism of catalysis by type-II NADH:quinone oxidoreductases. Sci. Rep., 7.","DOI":"10.1038\/srep40165"},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Yamashita, T., Inaoka, D.K., Shiba, T., Oohashi, T., Iwata, S., Yagi, T., Kosaka, T., Miyoshi, H., Harada, S., and Kita, K. (2018). Ubiquinone binding site of yeast NADH dehydrogenase revealed by structures binding novel competitive- and mixed-type inhibitors. Sci. Rep., 8.","DOI":"10.1038\/s41598-018-20775-6"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1021\/acsinfecdis.1c00413","article-title":"Synthesis and in vitro biological evaluation of quinolinyl pyrimidines targeting type II NADH-dehydrogenases (NDH-2)","volume":"8","author":"Lu","year":"2022","journal-title":"ACS Infect. Dis."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"3699","DOI":"10.1021\/acsinfecdis.4c00710","article-title":"2-Aryl-benzoimidazoles as type II NADH dehydrogenase inhibitors of Mycobacterium tuberculosis","volume":"10","author":"Saha","year":"2024","journal-title":"ACS Infect. Dis."},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Ke, H., Ganesan, S.M., Dass, S., Morrisey, J.M., Pou, S., Nilsen, A., Riscoe, M.K., Mather, M.W., and Vaidya, A.B. (2019). Mitochondrial type II NADH dehydrogenase of Plasmodium falciparum (PfNDH2) is dispensable in the asexual blood stages. PLoS ONE, 14.","DOI":"10.1371\/journal.pone.0214023"},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Lesanavi\u010dius, M., Aliverti, A., \u0160arlauskas, J., and \u010c\u0117nas, N. (2020). Reactions of Plasmodium falciparum ferredoxin:NADP+ oxidoreductase with redox cycling xenobiotics: A mechanistic study. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21093234"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1042\/bss0610171","article-title":"Radicals from one-electron reduction of nitro compounds, aromatic N-oxides and quinones: The kinetic basis for hypoxia-selective, bioreductive drugs","volume":"61","author":"Wardman","year":"1995","journal-title":"Biochem. Soc. Symp."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1128\/AAC.47.1.302-308.2003","article-title":"Reactivity of reduced [2Fe-2S] ferredoxin parallels host susceptibility to nitroimidazoles","volume":"47","author":"Vidakovic","year":"2003","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1042\/BJ20150650","article-title":"Nitroreductase gene-directed enzyme prodrug therapy: Insights and advances towards clinical utility","volume":"471","author":"Williams","year":"2015","journal-title":"Biochem. J."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"2851","DOI":"10.1021\/acs.jmedchem.8b00147","article-title":"Nitro-group-containing drugs","volume":"62","author":"Nepali","year":"2019","journal-title":"J. Med. Chem."},{"key":"ref_32","first-page":"174","article-title":"Diaziridinylbenzoquinones","volume":"382B","author":"Ward","year":"2004","journal-title":"Methods Enzymol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"2731","DOI":"10.1039\/b802649c","article-title":"The aza-analogues of 1,4-naphthoquinones are potent substrates and inhibitors of plasmodial thioredoxin and glutathione reductases and of human erythrocyte glutathione reductase","volume":"6","author":"Morin","year":"2008","journal-title":"Org. Biomol. Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"972","DOI":"10.1016\/j.bmcl.2008.11.071","article-title":"Type II NADH dehydrogenase of the respiratory chain of Plasmodium falciparum and its inhibitors","volume":"19","author":"Dong","year":"2009","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1637","DOI":"10.1063\/1.555843","article-title":"Reduction potentials of one-electron couples involving free radicals in aqueous solution","volume":"18","author":"Wardman","year":"1989","journal-title":"J. Phys. Chem. Ref. Data"},{"key":"ref_36","first-page":"258","article-title":"Structure-activity relationships in two-electron reduction of quinones","volume":"382B","author":"Nivinskas","year":"2004","journal-title":"Methods Enzymol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1042\/bj2570561","article-title":"DT-diaphorase-catalyzed reduction of 1,4-naphthoquinone derivatives and glutathionyl-quinone conjugates. Effects of substituents on autoxidation rates","volume":"257","author":"Buffinton","year":"1989","journal-title":"Biochem. J."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0009-2797(91)90029-7","article-title":"Molecular mechanisms of quinone cytotoxicity","volume":"80","year":"1991","journal-title":"Chem. Biol. Interact."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/S0003-9861(02)00228-X","article-title":"Two-electron reduction of quinones by Entero Enterobacter cloacae NAD(P)H:nitroreductase: Quantitative structure-activity relationships","volume":"403","author":"Nivinskas","year":"2002","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"259","DOI":"10.3109\/10715769009053359","article-title":"On the mechanism of one-electron reduction of quinones by microsomal flavin enzymes. The kinetic analysis between cytochrome b5 and menadione","volume":"8","author":"Iyanagi","year":"1990","journal-title":"Free Radic. Res. Commun."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1006\/bbrc.1996.0443","article-title":"Elimination of nitrite from the explosive 2,4,6-trinitrophenylmethylnitramine (tetryl) catalyzed by ferredoxin NADP+ oxidoreductase from spinach","volume":"220","author":"Shah","year":"1996","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1002\/jcc.21334","article-title":"AutoDoc Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading","volume":"31","author":"Trott","year":"2010","journal-title":"J. Comput. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1186\/s13321-021-00522-2","article-title":"GNINA 1:0: Molecular docking with deap learning","volume":"13","author":"McNutt","year":"2021","journal-title":"J. Cheminform."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"2601","DOI":"10.1042\/BCJ20210160","article-title":"The structures of E. coli NfsA bound to the antibiotic nitrofurantoin, to 1,4-benzoquinone and to FMN","volume":"478","author":"Day","year":"2021","journal-title":"Biochem. J."},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Valiauga, B., Bagd\u017ei\u016bnas, G., Sharrock, A.V., Ackerley, D.F., and \u010c\u0117nas, N. (2024). The catalysis mechanism of E. coli nitroreductase A, a candidate for gene-directed prodrug therapy: Potentiometric and substrate specificity studies. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms25084413"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"5578","DOI":"10.1016\/S0021-9258(18)61848-4","article-title":"Yeast glutathione reductase II. Interaction of oxidized and 2-electron reduced enzyme with reduced and oxidized nicotinamide adenine dinucleotide phosphate","volume":"246","author":"Bulger","year":"1971","journal-title":"J. Biol. Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/S0167-4838(97)00190-8","article-title":"Interaction of quinones with Arabidopsis thaliana thioredoxin reductase","volume":"1383","author":"Jacquot","year":"1998","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"2722","DOI":"10.1021\/acs.biochem.6b00070","article-title":"Substrate-protein interactions of type II NADH:quinone oxidoreductase from Escherichia coli","volume":"55","author":"Salewski","year":"2016","journal-title":"Biochemistry"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/0076-6879(79)63006-9","article-title":"Derivation and initial velocity and isotope exchange rate equations","volume":"63","author":"Huang","year":"1979","journal-title":"Methods Enzymol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.abb.2006.10.023","article-title":"Catalytic mechanism of hydride transfer between NADP+\/H and ferredoxin-NADP+ reductase from Anabaena PCC 7119","volume":"459","author":"Tejero","year":"2007","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"\u010c\u0117nas, N., Nemeikait\u0117-\u010c\u0117nien\u0117, A., and Kosychova, L. (2021). Single- and two-electron reduction of nitroaromatic compounds by flavoezymes: Mechanisms and implications for cytotoxicity. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22168534"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/0304-4173(85)90014-X","article-title":"Electron transfers in chemistry and biology","volume":"811","author":"Marcus","year":"1985","journal-title":"Biochim. Biophys. Acta-Rev. Bioenerg."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/S0076-6879(04)82009-3","article-title":"Structure and mechanism of NAD(P)H:quinone acceptor oxidoreductases (NQO)","volume":"382B","author":"Bianchet","year":"2004","journal-title":"Methods Enzymol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"18105","DOI":"10.1039\/C9CP02645B","article-title":"The global motion affecting electron transfer in Plasmodium falciparum type II NADH dehydrogenase: A novel non-competitive mechanism for quinolone ketone derivative inhibitors","volume":"21","author":"Xie","year":"2019","journal-title":"Phys. Chem. Chem. Phys."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S0014-5793(02)02881-8","article-title":"Does chloroquine really act through oxidative stress?","volume":"522","author":"Monti","year":"2002","journal-title":"FEBS Lett."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.ijpara.2003.09.011","article-title":"Oxidative stress in malaria parasite-infected erythrocytes: Host-parasite interactions","volume":"34","author":"Becker","year":"2004","journal-title":"Int. J. Parasitol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/S0304-4165(01)00169-6","article-title":"Quantitative structure-activity relationships in enzymatic single-electron reduction of nitroaromatic explosives: Implications for their cytotoxicity","volume":"1528","author":"Nivinskas","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_58","first-page":"414","article-title":"Determination of nitrite in water","volume":"86","author":"Montgomery","year":"1961","journal-title":"Analyst"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"e4792","DOI":"10.1002\/pro.4792","article-title":"CSF ChimeraX: Tools for structural building and analysis","volume":"32","author":"Meng","year":"2023","journal-title":"Protein Sci."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"D1373","DOI":"10.1093\/nar\/gkac956","article-title":"Pubchem 2023 update","volume":"51","author":"Kim","year":"2023","journal-title":"Nucleic Acids Res."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1002\/(SICI)1096-987X(199905)20:7<720::AID-JCC7>3.0.CO;2-X","article-title":"MMFFVI, MMFF94s options for energy minimization studies","volume":"20","author":"Halgren","year":"1999","journal-title":"J. Comput. Chem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1186\/1758-2946-4-17","article-title":"Avogadro: An advance semantic chemical editor, visualization, and analysis platform","volume":"4","author":"Hanwell","year":"2012","journal-title":"J. Cheminform."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"2785","DOI":"10.1002\/jcc.21256","article-title":"AutoDock4 and AutoDockTools4: Automated doc king with selective receptor flexibility","volume":"30","author":"Moriss","year":"2009","journal-title":"J. Comput. Chem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1186\/1758-2946-3-33","article-title":"Oper Babel: An open chemical toolbox","volume":"3","author":"Banck","year":"2011","journal-title":"J. Cheminform."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1186\/s13321-019-0362-7","article-title":"DockRMSD: An open-source tool for atom mapping and RMSD calculation of symmetric molecules","volume":"11","author":"Bell","year":"2019","journal-title":"J. Cheminform."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1002\/jcc.23538","article-title":"Voronota: A fast and reliable tool for computing the vertices of the Voronoi diagram of atomic balls","volume":"35","author":"Venclovas","year":"2014","journal-title":"J. Comput. Chem."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1893","DOI":"10.1021\/ci300604z","article-title":"Lesons learned in empirical scoring with smina from the CSAR 2011","volume":"53","author":"Koes","year":"2013","journal-title":"J. Chem. Inf. 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