{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,5]],"date-time":"2026-09-05T05:17:17Z","timestamp":1788585437243,"version":"build-2803163510"},"reference-count":29,"publisher":"The Society for Free Radical Research Japan","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J. Clin. Biochem. Nutr."],"published-print":{"date-parts":[[2026,9,1]]},"DOI":"10.3164\/jcbn.26-99","type":"journal-article","created":{"date-parts":[[2026,7,28]],"date-time":"2026-07-28T22:12:23Z","timestamp":1785276743000},"page":"163-169","source":"Crossref","is-referenced-by-count":0,"title":["Chemical generation of superoxide in the co-presence of riboflavin derivatives and NADH: evidence for a non-enzymatic redox pathway"],"prefix":"10.3164","volume":"79","author":[{"given":"Rinka","family":"Sugita","sequence":"first","affiliation":[{"name":"School of Bioscience and Biotechnology, Tokyo University of Technology"},{"name":"CIEL Co., Ltd."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sayaka","family":"Iida","sequence":"additional","affiliation":[{"name":"School of Bioscience and Biotechnology, Tokyo University of Technology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Midori","family":"Nagase","sequence":"additional","affiliation":[{"name":"School of Bioscience and Biotechnology, Tokyo University of Technology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hitoshi","family":"Masaki","sequence":"additional","affiliation":[{"name":"CIEL Co., Ltd."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yorihiro","family":"Yamamoto","sequence":"additional","affiliation":[{"name":"School of Bioscience and Biotechnology, Tokyo University of Technology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Akio","family":"Fujisawa","sequence":"additional","affiliation":[{"name":"School of Bioscience and Biotechnology, Tokyo University of Technology"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1739","reference":[{"key":"1","doi-asserted-by":"crossref","unstructured":"1 Yan LJ. Positive oxidative stress in aging and aging-related disease tolerance. Redox Biol 2014; 2: 165\u2013169.","DOI":"10.1016\/j.redox.2014.01.002"},{"key":"2","doi-asserted-by":"crossref","unstructured":"2 Kudryavtseva AV, Krasnov GS, Dmitriev AA, et al. Mitochondrial dysfunction and oxidative stress in aging and cancer. Oncotarget 2016; 7: 44879\u201344905.","DOI":"10.18632\/oncotarget.9821"},{"key":"3","doi-asserted-by":"crossref","unstructured":"3 Vatner SF, Zhang J, Oydanich M, Berkman T, Naftalovich R, Vatner DE. Healthful aging mediated by inhibition of oxidative stress. Ageing Res Rev 2020; 64: 101194.","DOI":"10.1016\/j.arr.2020.101194"},{"key":"4","doi-asserted-by":"crossref","unstructured":"4 Rosen DR, Siddique T, Patterson D, et al. Mutations in Cu\/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 1993; 362: 59\u201362.","DOI":"10.1038\/362059a0"},{"key":"5","doi-asserted-by":"crossref","unstructured":"5 Chen Z, Zhong C. Oxidative stress in Alzheimer\u2019s disease. Neurosci Bull 2014; 30: 271\u2013281.","DOI":"10.1007\/s12264-013-1423-y"},{"key":"6","doi-asserted-by":"crossref","unstructured":"6 Jellinger KA. Multiple system atrophy: an oligodendroglioneural synucleinopathy. J Alzheimers Dis 2018; 62: 1141\u20131179.","DOI":"10.3233\/JAD-170397"},{"key":"7","doi-asserted-by":"crossref","unstructured":"7 Hollen C, Neilson LE, Barajas RF Jr, Greenhouse I, Spain RI. Oxidative stress in multiple sclerosis\u2014Emerging imaging techniques. Front Neurol 2023; 13: 1025659.","DOI":"10.3389\/fneur.2022.1025659"},{"key":"8","doi-asserted-by":"crossref","unstructured":"8 Lee SS, Yoo YC. NOX-NOS crosstalk in the liver-brain axis: novel insights for redox regulation and neurodegenerative diseases. Redox Biol 2025; 86: 103807.","DOI":"10.1016\/j.redox.2025.103807"},{"key":"9","doi-asserted-by":"crossref","unstructured":"9 Reuter S, Gupta SC, Chaturvedi MM, Aggarwal BB. Oxidative stress, inflammation, and cancer: How are they linked? Free Radic Biol Med 2010; 49: 1603\u20131616.","DOI":"10.1016\/j.freeradbiomed.2010.09.006"},{"key":"10","doi-asserted-by":"crossref","unstructured":"10 Aleksandrova K, Koelman L, Rodrigues CE. Dietary patterns and biomarkers of oxidative stress and inflammation: a systematic review of observational and intervention studies. Redox Biol 2021; 42: 101869.","DOI":"10.1016\/j.redox.2021.101869"},{"key":"11","doi-asserted-by":"crossref","unstructured":"11 Weinberg Sibony R, Segev O, Dor S, Raz I. Overview of oxidative stress and inflammation in diabetes. J Diabetes 2024; 16: e70014.","DOI":"10.1111\/1753-0407.70014"},{"key":"12","doi-asserted-by":"crossref","unstructured":"12 Meng L, Liu S, Luo J, et al. Oxidative stress and reactive oxygen species in otorhinolaryngological diseases: insights from pathophysiology to targeted antioxidant therapies. Redox Rep 2025; 30: 2458942.","DOI":"10.1080\/13510002.2025.2458942"},{"key":"13","doi-asserted-by":"crossref","unstructured":"13 Bugger H, Pfeil K. Mitochondrial ROS in myocardial ischemia reperfusion and remodeling. Biochim Biophys Acta Mol Basis Dis 2020; 1866: 165768.","DOI":"10.1016\/j.bbadis.2020.165768"},{"key":"14","doi-asserted-by":"crossref","unstructured":"14 Xiang M, Lu Y, Xin L, et al. Role of oxidative stress in reperfusion following myocardial ischemia and its treatments. Oxid Med Cell Longev 2021; 2021: 6614009.","DOI":"10.1155\/2021\/6614009"},{"key":"15","doi-asserted-by":"crossref","unstructured":"15 George J, Lu Y, Tsuchishima M, Tsutsumi M. Cellular and molecular mechanisms of hepatic ischemia-reperfusion injury: the role of oxidative stress and therapeutic approaches. Redox Biol 2024; 75: 103258.","DOI":"10.1016\/j.redox.2024.103258"},{"key":"16","doi-asserted-by":"crossref","unstructured":"16 Shimizu R, Watanabe H, Iida S, Yamamoto Y, Fujisawa A. Formation of singlet oxygen in addition to hydroxyl radical via the Fenton reaction. Redox Biol 2025; 84: 103687.","DOI":"10.1016\/j.redox.2025.103687"},{"key":"17","doi-asserted-by":"crossref","unstructured":"17 Blough NV, Zafiriou OC. Reaction of superoxide with nitric oxide to form peroxonitrite in alkaline aqueous solution. Inorg Chem 1985; 24: 3502\u20133504.","DOI":"10.1021\/ic00216a003"},{"key":"18","doi-asserted-by":"crossref","unstructured":"18 Nagase M, Sakamoto M, Amekura S, et al. Riboflavin compounds show NAD(P)H dependent quinone oxidoreductase-like quinone reducing activity. J Clin Biochem Nutr 2023; 73: 52\u201360.","DOI":"10.3164\/jcbn.22-140"},{"key":"19","doi-asserted-by":"crossref","unstructured":"19 McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 1969; 244: 6049\u20136055.","DOI":"10.1016\/S0021-9258(18)63504-5"},{"key":"20","doi-asserted-by":"crossref","unstructured":"20 Pakiari AH, Salarhaji M, Abdollahi T, Safapour M. The redox potential of flavin derivatives as a mediator in biosensors. J Mol Model 2021; 27: 96.","DOI":"10.1007\/s00894-020-04650-8"},{"key":"21","doi-asserted-by":"crossref","unstructured":"21 Finn RD, Basran J, Roitel O, et al. Determination of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1. Eur J Biochem 2003; 270: 1164\u20131175.","DOI":"10.1046\/j.1432-1033.2003.03474.x"},{"key":"22","doi-asserted-by":"crossref","unstructured":"22 Wood PM. The potential diagram for oxygen at pH 7. Biochem J 1988; 253: 287\u2013289.","DOI":"10.1042\/bj2530287"},{"key":"23","doi-asserted-by":"crossref","unstructured":"23 Chaiyen P, Fraaije MW, Mattevi A. The enigmatic reaction of flavins with oxygen. Trends Biochem Sci 2012; 37: 373\u2013380.","DOI":"10.1016\/j.tibs.2012.06.005"},{"key":"24","doi-asserted-by":"crossref","unstructured":"24 Bailey MR, Schultz ZD. SERS speciation of the electrochemical oxidation-reduction of riboflavin. Analyst 2016; 141: 5078\u20135087.","DOI":"10.1039\/C6AN01054G"},{"key":"25","doi-asserted-by":"crossref","unstructured":"25 Austvold CK, Keable SM, Procopio M, Usselman RJ. Quantitative measurements of reactive oxygen species partitioning in electron transfer flavoenzyme magnetic field sensing. Front Physiol 2024; 15: 1348395.","DOI":"10.3389\/fphys.2024.1348395"},{"key":"26","doi-asserted-by":"crossref","unstructured":"26 Ngo MA, Sinitsyna NN, Qin Q, Rice RH. Oxygen-dependent differentiation of human keratinocytes. J Invest Dermatol 2007; 127: 354\u2013361.","DOI":"10.1038\/sj.jid.5700522"},{"key":"27","doi-asserted-by":"crossref","unstructured":"27 Treberg JR, Quinlan CL, Brand MD. Evidence for two sites of superoxide production by mitochondrial NADH-ubiquinone oxidoreductase (complex I). J Biol Chem 2011; 286: 27103\u201327110.","DOI":"10.1074\/jbc.M111.252502"},{"key":"28","doi-asserted-by":"crossref","unstructured":"28 Lambert AJ, Brand MD. Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane. Biochem J 2004; 382 (Pt 2): 511\u2013517.","DOI":"10.1042\/BJ20040485"},{"key":"29","doi-asserted-by":"crossref","unstructured":"29 Chen YR, Chen CL, Zhang L, Green-Church KB, Zweier JL. Superoxide generation from mitochondrial NADH dehydrogenase induces self-inactivation with specific protein radical formation. J Biol Chem 2005; 280: 37339\u201337348.","DOI":"10.1074\/jbc.M503936200"}],"container-title":["Journal of Clinical Biochemistry and Nutrition"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/jcbn\/79\/2\/79_26-99\/_pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,5]],"date-time":"2026-09-05T04:50:19Z","timestamp":1788583819000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/jcbn\/79\/2\/79_26-99\/_article"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,1]]},"references-count":29,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2026]]}},"URL":"https:\/\/doi.org\/10.3164\/jcbn.26-99","relation":{},"ISSN":["0912-0009","1880-5086"],"issn-type":[{"value":"0912-0009","type":"print"},{"value":"1880-5086","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,1]]},"article-number":"26-99"}}