{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,12]],"date-time":"2025-11-12T06:31:31Z","timestamp":1762929091812,"version":"build-2065373602"},"reference-count":68,"publisher":"MDPI AG","issue":"13","license":[{"start":{"date-parts":[[2024,6,29]],"date-time":"2024-06-29T00:00:00Z","timestamp":1719619200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100006769","name":"Russian Science Foundation","doi-asserted-by":"publisher","award":["24-24-00210"],"award-info":[{"award-number":["24-24-00210"]}],"id":[{"id":"10.13039\/501100006769","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Nitrosyl iron complexes are remarkably multifactorial pharmacological agents. These compounds have been proven to be particularly effective in treating cardiovascular and oncological diseases. We evaluated and compared the antioxidant activity of tetranitrosyl iron complexes (TNICs) with thiosulfate ligands and dinitrosyl iron complexes (DNICs) with glutathione (DNIC-GS) or phosphate (DNIC-PO4\u2212) ligands in hemoglobin-containing systems. The studied effects included the production of free radical intermediates during hemoglobin (Hb) oxidation by tert-butyl hydroperoxide, oxidative modification of Hb, and antioxidant properties of nitrosyl iron complexes. Measuring luminol chemiluminescence revealed that the antioxidant effect of TNICs was higher compared to DNIC-PO4\u2212. DNIC-GS either did not exhibit antioxidant activity or exerted prooxidant effects at certain concentrations, which might have resulted from thiyl radical formation. TNICs and DNIC-PO4\u2212 efficiently protected the Hb heme group from decomposition by organic hydroperoxides. DNIC-GS did not exert any protective effects on the heme group; however, it abolished oxoferrylHb generation. TNICs inhibited the formation of Hb multimeric forms more efficiently than DNICs. Thus, TNICs had more pronounced antioxidant activity than DNICs in Hb-containing systems.<\/jats:p>","DOI":"10.3390\/ijms25137194","type":"journal-article","created":{"date-parts":[[2024,7,2]],"date-time":"2024-07-02T12:58:42Z","timestamp":1719925122000},"page":"7194","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Effects of Nitrosyl Iron Complexes with Thiol, Phosphate, and Thiosulfate Ligands on Hemoglobin"],"prefix":"10.3390","volume":"25","author":[{"given":"Olga V.","family":"Kosmachevskaya","sequence":"first","affiliation":[{"name":"Bach Institute of Biochemistry, Federal Research Center of Biotechnology, Russian Academy of Sciences, Moscow 119071, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elvira I.","family":"Nasybullina","sequence":"additional","affiliation":[{"name":"Bach Institute of Biochemistry, Federal Research Center of Biotechnology, Russian Academy of Sciences, Moscow 119071, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Olesya V.","family":"Pokidova","sequence":"additional","affiliation":[{"name":"Federal Research Center of Problems of Chemical Physics and Medicinal Chemistry, Russian Academy of Sciences, Moscow Region, Chernogolovka 142432, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5344-6220","authenticated-orcid":false,"given":"Natalia A.","family":"Sanina","sequence":"additional","affiliation":[{"name":"Federal Research Center of Problems of Chemical Physics and Medicinal Chemistry, Russian Academy of Sciences, Moscow Region, Chernogolovka 142432, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6625-7373","authenticated-orcid":false,"given":"Alexey F.","family":"Topunov","sequence":"additional","affiliation":[{"name":"Bach Institute of Biochemistry, Federal Research Center of Biotechnology, Russian Academy of Sciences, Moscow 119071, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2024,6,29]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"8273","DOI":"10.1039\/c0dt01244k","article-title":"Nitrosyl iron complexes\u2014Synthesis, structure and biology","volume":"40","author":"Lewandowska","year":"2011","journal-title":"Dalton Trans."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"2853","DOI":"10.1016\/j.cell.2022.06.010","article-title":"Nitric oxide signaling in health and disease","volume":"185","author":"Lundberg","year":"2022","journal-title":"Cell"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"1338","DOI":"10.1021\/acs.chemrev.7b00568","article-title":"Biochemistry of peroxynitrite and protein tyrosine nitration","volume":"118","author":"Campolo","year":"2018","journal-title":"Chem. Rev."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1016\/j.bcp.2019.04.021","article-title":"Sulodexide promotes arterial relaxation via endothelium-dependent nitric oxide-mediated pathway","volume":"166","author":"Raffetto","year":"2019","journal-title":"Biochem. Pharmacol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1016\/j.cellsig.2018.10.019","article-title":"Nitric oxide mediated redox regulation of protein homeostasis","volume":"53","author":"Tegeder","year":"2019","journal-title":"Cell. Signal."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"118377","DOI":"10.1016\/j.lfs.2020.118377","article-title":"Functional implications of vascular endothelium in regulation of endothelial nitric oxide synthesis to control blood pressure and cardiac functions","volume":"259","author":"Kumar","year":"2020","journal-title":"Life Sci."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"8935","DOI":"10.1021\/acsnano.3c02303","article-title":"Advanced nitric oxide generating nanomedicine for therapeutic applications","volume":"17","author":"Wang","year":"2023","journal-title":"ACS Nano"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1016\/j.biopha.2017.10.122","article-title":"Nitric oxide bioavailability dysfunction involves in atherosclerosis","volume":"97","author":"Chen","year":"2018","journal-title":"Biomed. Pharmacother."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"100084","DOI":"10.1016\/j.hsr.2023.100084","article-title":"Endothelial dysfunction and its relation in different disorders: Recent update","volume":"7","author":"Ray","year":"2023","journal-title":"Health Sci. Rev."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1774","DOI":"10.2174\/138161211796391047","article-title":"Nitric oxide and protection against cardiac ischemia","volume":"17","author":"Xia","year":"2011","journal-title":"Curr. Pharm. Des."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1007\/s00424-018-02251-2","article-title":"Protective efficacy of dinitrosyl iron complexes with reduced glutathione in cardioplegia and reperfusion","volume":"471","author":"Pisarenko","year":"2019","journal-title":"Pflug. Arch."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"133506","DOI":"10.1016\/j.molstruc.2022.133506","article-title":"Anionic dinitrosyl iron complexes\u2014New nitric oxide donors with selective toxicity to human glioblastoma cells","volume":"1266","author":"Sanina","year":"2022","journal-title":"J. Mol. Struct."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1007\/s11172-023-3872-9","article-title":"Effect of the dinitrosyl iron complex with N-ethylthiourea on ROS and NO intracellular levels and caspase activity in HeLa tumor cells","volume":"72","author":"Amozova","year":"2023","journal-title":"Russ. Chem. Bull."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"7063","DOI":"10.1039\/D1TB00847A","article-title":"Recent advances in the development of nitric oxide-releasing biomaterials and their application potentials in chronic wound healing","volume":"9","author":"Wu","year":"2021","journal-title":"J. Mater. Chem. B"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1039\/D0NR07484E","article-title":"Advanced nitric oxide donors: Chemical structure of NO drugs, NO nanomedicines and biomedical applications","volume":"13","author":"Yang","year":"2021","journal-title":"Nanoscale"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1022","DOI":"10.1039\/C4NJ01693A","article-title":"Nitrosyl iron complexes with enhanced NO donating ability: Synthesis, structure and properties of a new type of salt with the DNIC cations [Fe(SC(NH2)2)2(NO)2]+","volume":"39","author":"Sanina","year":"2015","journal-title":"New J. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Ahmed, R., Augustine, R., Chaudhry, M., Akhtar, U.A., Zahid, A.A., Tariq, M., Falahati, M., Ahmad, I.S., and Hasan, A. (2022). Nitric oxide-releasing biomaterials for promoting wound healing in impaired diabetic wounds: State of the art and recent trends. Biomed. Pharmacother., 149.","DOI":"10.1016\/j.biopha.2022.112707"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1016\/j.niox.2006.12.003","article-title":"Vasorelaxing activity of stable powder preparations of dinitrosyl iron complexes with cysteine or glutathione ligands","volume":"16","author":"Vanin","year":"2007","journal-title":"Nitric Oxide"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1367","DOI":"10.1134\/S0006297922110153","article-title":"Positive (regulatory) and negative (cytotoxic) effects of dinitrosyl iron complexes on living organisms","volume":"87","author":"Vanin","year":"2022","journal-title":"Biochemistry (Moscow)"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"11451","DOI":"10.1039\/D0DT02135K","article-title":"Recent advances in iron-complexes as drug candidates for cancer therapy: Reactivity, mechanism of action and metabolites","volume":"49","author":"Hognon","year":"2020","journal-title":"Dalton Trans."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"15846","DOI":"10.1021\/acs.inorgchem.1c00566","article-title":"Insight into the electronic structure of biomimetic dinitrosyliron complexes (DNICs): Toward the syntheses of amido-bridging dinuclear DNICs","volume":"60","author":"Lu","year":"2021","journal-title":"Inorg. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"2922","DOI":"10.1021\/acschemneuro.3c00348","article-title":"Neuroprotective effect of NO-delivery dinitrosyl iron complexes (DNICs) on amyloid pathology in the Alzheimer\u2019s disease cell model","volume":"14","author":"Chuang","year":"2023","journal-title":"ACS Chem. Neurosci."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1002\/jccs.202300002","article-title":"Light-induced NO release from iron-nitrosyl-thiolato complex: The role of noncovalent thiol\/thioether","volume":"70","author":"Chen","year":"2023","journal-title":"J. Chin. Chem. Soc."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"119369","DOI":"10.1016\/j.ica.2019.119369","article-title":"Decomposition of the binuclear nitrosyl iron complex with thiosulfato ligands in aqueous solutions: Experimental and theoretical study","volume":"502","author":"Pokidova","year":"2020","journal-title":"Inorganica Chim. Acta"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/0003-9861(91)90452-O","article-title":"Nitric oxide as an antioxidant","volume":"289","author":"Kanner","year":"1991","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1016\/S0891-5849(98)00092-6","article-title":"Chemical biology of nitric oxide: Insights into regulatory, cytotoxic, and cytoprotective mechanisms of nitric oxide","volume":"25","author":"Wink","year":"1998","journal-title":"Free Radic. Biol. Med."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"6689","DOI":"10.1021\/bi00020a014","article-title":"Reduction of ferrylmyoglobin and ferrylhemoglobin by nitric oxide: A protective mechanism against ferryl hemoprotein-induced oxidations","volume":"34","author":"Gorbunov","year":"1995","journal-title":"Biochemistry"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1006\/bbrc.1997.7951","article-title":"Nitric oxide protects cardiomyocytes against tert-butyl hydroperoxide-induced formation of alkoxyl and peroxyl radicals and peroxidation of phosphatidylserine","volume":"244","author":"Gorbunov","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1016\/S0005-2728(99)00027-4","article-title":"Nitric oxide and lipid peroxidation","volume":"1411","author":"Hogg","year":"1999","journal-title":"Biochim. Biophys. Acta (BBA)-Bioenerg."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1023\/B:BIRY.0000029856.67884.c5","article-title":"Interaction of oxoferrylmyoglobin and dinitrosyl-iron complexes","volume":"69","author":"Shumaev","year":"2004","journal-title":"Biochemistry (Moscow)"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/S0076-6879(08)36025-X","article-title":"Dinitrosyl iron complexes bind with hemoglobin as markers of oxidative stress","volume":"436","author":"Shumaev","year":"2008","journal-title":"Methods Enzymol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"2798154","DOI":"10.1155\/2019\/2798154","article-title":"Protective effect of dinitrosyl iron complexes with glutathione in red blood cell lysis induced by hypochlorous acid","volume":"2019","author":"Shumaev","year":"2019","journal-title":"Oxid. Med. Cell. Longev."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1016\/j.freeradbiomed.2005.08.047","article-title":"Nitric oxide as a cellular antioxidant: A little goes a long way","volume":"40","author":"Hummel","year":"2006","journal-title":"Free Radic. Biol. Med."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.niox.2018.03.003","article-title":"Nitric oxide reduces oxidative stress in cancers cells by forming dinitrosyliron complexes","volume":"76","author":"Sahni","year":"2018","journal-title":"Nitric Oxide"},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Kosmachevskaya, O.V., Nasybullina, E.I., Shumaev, K.B., Novikova, N.N., and Topunov, A.F. (2021). Protective effect of dinitrosyl iron complexes bound with hemoglobin on oxidative modification by peroxynitrite. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms222413649"},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Vlasova, I.I. (2018). Peroxidase activity of human hemoproteins: Keeping the fire under control. Molecules, 23.","DOI":"10.3390\/molecules23102561"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"2473","DOI":"10.1039\/c0ob00876a","article-title":"DEPMPO: An efficient tool for the coupled ESR-spin trapping of alkylperoxyl radicals in water","volume":"9","author":"Karoui","year":"2011","journal-title":"Org. Biomol. Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"6000","DOI":"10.1074\/jbc.271.11.6000","article-title":"Characterization of sulfur-centered radical intermediates formed during the oxidation of thiols and sulfite by peroxynitrite. ESR-spin trapping and oxygen uptake studies","volume":"271","author":"Karoui","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_39","first-page":"954","article-title":"The radical and redox chemistry of myoglobin and hemoglobin: From in vitro studies to human pathology","volume":"6","author":"Reeder","year":"2004","journal-title":"Antioxid. Redox Signal."},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Kosmachevskaya, O.V., Nasybullina, E.I., Pugachenko, I.S., Novikova, N.N., and Topunov, A.F. (2022). Antiglycation and antioxidant effect of nitroxyl towards hemoglobin. Antioxidants, 11.","DOI":"10.3390\/antiox11102007"},{"key":"ref_41","first-page":"80","article-title":"Inhibition of formation of conjugated dienes in linseed oil","volume":"72","year":"2018","journal-title":"Proc. Latv. Acad. Sci. Sect. B"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1179","DOI":"10.1007\/s10534-011-9476-8","article-title":"Glutathione: A key component of the cytoplasmic labile iron pool","volume":"24","author":"Hider","year":"2011","journal-title":"Biometals"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"28926","DOI":"10.1074\/jbc.M707862200","article-title":"Nitric oxide-induced conversion of cellular chelatable iron into macromolecule-bound paramagnetic dinitrosyliron complexes","volume":"283","author":"Toledo","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"4671","DOI":"10.1073\/pnas.0710416106","article-title":"Dinitrosyliron complexes and the mechanism(s) of cellular protein nitrosothiol formation from nitric oxide","volume":"106","author":"Bosworth","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"2565","DOI":"10.1021\/ic011220w","article-title":"Mechanistic information on the reversible binding of NO to selected iron(II) chelates from activation parameters","volume":"41","author":"Schneppensieper","year":"2002","journal-title":"Inorg. Chem."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"19917","DOI":"10.1074\/jbc.M114.569764","article-title":"Nitrosothiol formation and protection against Fenton chemistry by nitric oxide-induced dinitrosyliron complex formation from anoxia-initiated cellular chelatable iron increase","volume":"289","author":"Li","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"9431","DOI":"10.1039\/C9DT00777F","article-title":"Villaflores Fe in biosynthesis, translocation, and signal transduction of NO: Toward bioinorganic engineering of dinitrosyl iron complexes into NO-delivery scaffolds for tissue engineering","volume":"48","author":"Hsiao","year":"2019","journal-title":"Dalton Trans."},{"key":"ref_48","unstructured":"Vanin, A.F. (2019). Dinitrosyl Iron Complexes as a \u201cWorking Form\u201d of Nitric Oxide in Living Organisms, Cambridge Scholars Publishing."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/j.redox.2013.12.027","article-title":"Endothelial nitric oxide synthase in red blood cells: Key to a new erythrocrine function?","volume":"2","author":"Kelm","year":"2014","journal-title":"Redox Biol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1021\/ar800089j","article-title":"The new chemical biology of nitrite reactions with hemoglobin: R-state catalysis, oxidative denitrosylation, and nitrite reductase\/anhydrase","volume":"42","author":"Gladwin","year":"2009","journal-title":"Acc. Chem. Res."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1111\/j.1749-6632.2002.tb04063.x","article-title":"Nitric oxide transport and storage in the cardiovascular system","volume":"962","author":"Muller","year":"2002","journal-title":"Ann. N.-Y. Acad. Sci."},{"key":"ref_52","first-page":"215","article-title":"Beneficial and harmful effects of thiols","volume":"54","year":"2002","journal-title":"Pol. J. Pharmacol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1184","DOI":"10.1021\/ja108313u","article-title":"Phenol nitration induced by an {Fe(NO)2}(10) dinitrosyl iron complex","volume":"133","author":"Tran","year":"2011","journal-title":"J. Am. Chem. Soc."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"4636","DOI":"10.1039\/c2cc31117h","article-title":"Reaction of a copper(II)\u2013nitrosyl complex with hydrogen peroxide: Putative formation of a copper(I)\u2013peroxynitrite intermediate","volume":"48","author":"Kalita","year":"2012","journal-title":"Chem. Commun."},{"key":"ref_55","first-page":"153","article-title":"Interaction of peroxynitrite and hydrogen peroxide with dinitrosyl iron complexes containing thiol ligands in vitro","volume":"64","author":"Lobysheva","year":"1999","journal-title":"Biochemistry (Moscow)"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"13194","DOI":"10.1021\/bi980941c","article-title":"Superoxide produced in the heme pocket of the beta-chain of hemoglobin reacts with the beta-93 cysteine to produce a thiyl radical","volume":"37","author":"Balagopalakrishna","year":"1998","journal-title":"Biochemistry"},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Rubino, F.M. (2021). The redox potential of the \u03b2-93-cysteine thiol group in human hemoglobin estimated from in vitro oxidant challenge experiments. Molecules, 26.","DOI":"10.3390\/molecules26092528"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.freeradbiomed.2012.11.003","article-title":"Antioxidant functions for the hemoglobin \u03b293 cysteine residue in erythrocytes and in the vascular compartment in vivo","volume":"55","author":"Vitturi","year":"2013","journal-title":"Free Radic. Biol. Med."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"9456163","DOI":"10.1155\/2017\/9456163","article-title":"Protective effects of dinitrosyl iron complexes under oxidative stress in the heart","volume":"2017","author":"Kapelko","year":"2017","journal-title":"Oxid. Med. Cell. Longev."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1016\/j.freeradbiomed.2015.08.012","article-title":"The cytoprotective effect of nitrite is based on the formation of dinitrosyl iron complexes","volume":"89","author":"Dungel","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"ref_61","doi-asserted-by":"crossref","unstructured":"Akentieva, N.P., Sanina, N.A., Gizatullin, A.R., Shkondina, N.I., Prikhodchenko, T.R., Shram, S.I., Zhelev, N., and Aldoshin, S.M. (2019). Cytoprotective effects of dinitrosyl iron complexes on viability of human fibroblasts and cardiomyocytes. Front. Pharmacol., 10.","DOI":"10.3389\/fphar.2019.01277"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"6473","DOI":"10.1039\/D2DT00291D","article-title":"Albumin as prospective carrier of nitrosyl iron complex with thiourea and thiosulfate ligands under aerobic conditions","volume":"51","author":"Pokidova","year":"2022","journal-title":"Dalton Trans."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1038\/nature03609","article-title":"Structure of oxidized alpha-haemoglobin bound to AHSP reveals a protective mechanism for haem","volume":"435","author":"Feng","year":"2005","journal-title":"Nature"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1016\/S0891-5849(98)00315-3","article-title":"Antioxidant activity applying an improved ABTS radical cation decolorization assay","volume":"26","author":"Re","year":"1999","journal-title":"Free Radic. Biol. Med."},{"key":"ref_65","doi-asserted-by":"crossref","unstructured":"Ilyasov, I.R., Beloborodov, V.L., Selivanova, I.A., and Terekhov, R.P. (2020). ABTS\/PP decolorization assay of antioxidant capacity reaction pathways. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21031131"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/0076-6879(81)76111-1","article-title":"Preparation of blood hemoglobins of vertebrates","volume":"76","author":"Riggs","year":"1981","journal-title":"Methods Enzymol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Kosmachevskaya, O.V., Novikova, N.N., and Topunov, A.F. (2021). Carbonyl stress in red blood cells and hemoglobin. Antioxidants, 10.","DOI":"10.3390\/antiox10020253"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/25\/13\/7194\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T15:07:50Z","timestamp":1760108870000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/25\/13\/7194"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,6,29]]},"references-count":68,"journal-issue":{"issue":"13","published-online":{"date-parts":[[2024,7]]}},"alternative-id":["ijms25137194"],"URL":"https:\/\/doi.org\/10.3390\/ijms25137194","relation":{},"ISSN":["1422-0067"],"issn-type":[{"type":"electronic","value":"1422-0067"}],"subject":[],"published":{"date-parts":[[2024,6,29]]}}}