{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,12]],"date-time":"2026-08-12T22:29:28Z","timestamp":1786573768401,"version":"build-2736575974"},"reference-count":78,"publisher":"MDPI AG","issue":"24","license":[{"start":{"date-parts":[[2021,12,20]],"date-time":"2021-12-20T00:00:00Z","timestamp":1639958400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100002261","name":"Russian Foundation for Basic Research","doi-asserted-by":"publisher","award":["19-29-12052; 19-015-00444"],"award-info":[{"award-number":["19-29-12052; 19-015-00444"]}],"id":[{"id":"10.13039\/501100002261","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Dinitrosyl iron complexes (DNICs) are a physiological form of nitric oxide (\u2022NO) in an organism. They are able not only to deposit and transport \u2022NO, but are also to act as antioxidant and antiradical agents. However, the mechanics of hemoglobin-bound DNICs (Hb-DNICs) protecting Hb against peroxynitrite-caused, mediated oxidative modification have not yet been scrutinized. Through EPR spectroscopy we show that Hb-DNICs are destroyed under the peroxynitrite action in a dose-dependent manner. At the same time, DNICs inhibit the oxidation of tryptophan and tyrosine residues and formation of carbonyl derivatives. They also prevent the formation of covalent crosslinks between Hb subunits and degradation of a heme group. These effects can arise from the oxoferryl heme form being reduced, and they can be connected with the ability of DNICs to directly intercept peroxynitrite and free radicals, which emerge due to its homolysis. These data show that DNICs may ensure protection from myocardial ischemia.<\/jats:p>","DOI":"10.3390\/ijms222413649","type":"journal-article","created":{"date-parts":[[2021,12,20]],"date-time":"2021-12-20T08:43:32Z","timestamp":1639989812000},"page":"13649","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Protective Effect of Dinitrosyl Iron Complexes Bound with Hemoglobin on Oxidative Modification by Peroxynitrite"],"prefix":"10.3390","volume":"22","author":[{"given":"Olga V.","family":"Kosmachevskaya","sequence":"first","affiliation":[{"name":"Research Center of Biotechnology of the Russian Academy of Sciences, Bach Institute of Biochemistry, 119071 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elvira I.","family":"Nasybullina","sequence":"additional","affiliation":[{"name":"Research Center of Biotechnology of the Russian Academy of Sciences, Bach Institute of Biochemistry, 119071 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Konstantin B.","family":"Shumaev","sequence":"additional","affiliation":[{"name":"Research Center of Biotechnology of the Russian Academy of Sciences, Bach Institute of Biochemistry, 119071 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natalia N.","family":"Novikova","sequence":"additional","affiliation":[{"name":"National Research Center, Kurchatov Institute, 123182 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6625-7373","authenticated-orcid":false,"given":"Alexey F.","family":"Topunov","sequence":"additional","affiliation":[{"name":"Research Center of Biotechnology of the Russian Academy of Sciences, Bach Institute of Biochemistry, 119071 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,12,20]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1184","DOI":"10.1021\/ar500459j","article-title":"Dinitrosyl iron complexes (DNICs): From biomimetic synthesis and spectroscopic characterization toward unveiling the biological and catalytic roles of DNICs","volume":"48","author":"Tsai","year":"2015","journal-title":"Acc. Chem. Res."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.niox.2016.01.006","article-title":"Dinitrosyl iron complexes with thiol-containing ligands as a \u201cworking form\u201d of endogenous nitric oxide","volume":"54","author":"Vanin","year":"2016","journal-title":"Nitric Oxide"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"9431","DOI":"10.1039\/C9DT00777F","article-title":"Fe in biosynthesis, translocations, 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_4","first-page":"298","article-title":"Dinitrosyl iron complexes\u2014Structure and biological functions","volume":"56","author":"Lewandowska","year":"2010","journal-title":"Post\u0119py Biochemii"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1007\/s12013-019-00886-1","article-title":"What is the mechanism of nitric oxide conversion into nitrosonium ions ensuriong S-nitrosating processes in living organisms","volume":"77","author":"Vanin","year":"2019","journal-title":"Cell Biochem. Biophys."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1006\/bbrc.1993.2079","article-title":"The reaction of nitric oxide with organic peroxyl radicals","volume":"195","author":"Padmaja","year":"1993","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1134\/S0003683820060022","article-title":"Peroxynitrite: Toxic agent and signaling molecule","volume":"56","author":"Abalenikhina","year":"2020","journal-title":"Appl. Biochem. Microbiol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"C1424","DOI":"10.1152\/ajpcell.1996.271.5.C1424","article-title":"Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and ugly","volume":"271","author":"Beckman","year":"1996","journal-title":"Am. J. Physiol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1021\/tx0496800","article-title":"The physiological chemistry and biological activity of nitroxyl (HNO): The neglected, misunderstood, and enigmatic nitrogen oxide","volume":"18","author":"Fukuto","year":"2005","journal-title":"Chem. Res. Toxicol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1152\/physrev.00029.2006","article-title":"Nitric oxide and peroxynitrite in health and disease","volume":"87","author":"Pacher","year":"2007","journal-title":"Physiol. Rev."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1016\/j.freeradbiomed.2015.06.027","article-title":"Nitric oxide diffusion to red blood cells limits extracellular, but not intraphagosomal, peroxynitrite formation by macrophages","volume":"87","author":"Prolo","year":"2015","journal-title":"Free Radic. Biol. Med."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"2099","DOI":"10.1172\/JCI24650","article-title":"Enzymatic function of hemoglobin as a nitrite reductase that produces NO under allosteric control","volume":"115","author":"Huang","year":"2005","journal-title":"J. Clin. Investig."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"6393","DOI":"10.1021\/bi952875+","article-title":"Production of superoxide from hemoglobin-bound oxygen under hypoxic conditions","volume":"35","author":"Balagopalakrishna","year":"1996","journal-title":"Biochemistry"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.niox.2007.09.085","article-title":"Interaction of reactive oxygen and nitrogen species with albumin\u2014And hemoglobin bound dinitrosyl iron complexes","volume":"18","author":"Shumaev","year":"2008","journal-title":"Nitric Oxide"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/S0076-6879(08)36025-X","article-title":"Dinitrosyl iron complexes bound with haemoglobin as markers of oxidative stress","volume":"436","author":"Shumaev","year":"2008","journal-title":"Methods Enzymol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1007\/s00726-003-0021-0","article-title":"Peroxynitrite-dependent modifications of tyrosine residues in hemoglobin. Formation of tyrosyl radical(s) and 3-nitrotyrosine","volume":"25","author":"Pietraforte","year":"2003","journal-title":"Amino Acids"},{"key":"ref_17","first-page":"569","article-title":"Interaction of oxoferrylmyoglobin and dinitrosyl iron complexes","volume":"69","author":"Shumaev","year":"2004","journal-title":"Biochemistry"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"e2798154","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_19","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1111\/j.1365-2958.2008.06464.x","article-title":"Nitric oxide-induced bacteriostasis ana modification of iron-sulphur proteins in Escherichia Coli","volume":"70","author":"Ren","year":"2008","journal-title":"Mol. Microbiol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1007\/s00726-003-0011-2","article-title":"Free radical-mediated oxidation of free amino acids and amino acid residues in proteins","volume":"25","author":"Stadtman","year":"2003","journal-title":"Amino Acids"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1042\/BJ20151227","article-title":"Protein oxidation and peroxidation","volume":"473","author":"Davies","year":"2016","journal-title":"Biochem. J."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1007\/s00726-003-0012-1","article-title":"Recent advances in the analysis of oxidized proteins","volume":"25","author":"Requena","year":"2003","journal-title":"Amino Acids"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1179\/1351000214Y.0000000099","article-title":"Metal-catalyzed protein tyrosine nitration in biological systems","volume":"19","author":"Campolo","year":"2014","journal-title":"Redox Rep."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1006\/bbrc.1998.8846","article-title":"Formation of fluorescent heme degradation products during the oxidation of hemoglobin by hydrogen peroxide","volume":"247","author":"Nagababu","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1021\/tx990201k","article-title":"Kinetic and mechanistic studies of the peroxynitrite-mediated oxidation of oxymyoglobin and oxyhemoglobin","volume":"13","author":"Exner","year":"2000","journal-title":"Chem. Res. Toxicol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1006\/abbi.1997.0449","article-title":"Peroxynitrite mediated heme oxidation and protein modification of native and chemically modified hemoglobins","volume":"349","author":"Alayash","year":"1998","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1002\/iub.149","article-title":"Catalytic peroxidation of nitrogen monoxide and peroxynitrite by globins","volume":"61","author":"Casella","year":"2009","journal-title":"IUBMB Life"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/S0891-5849(02)01355-2","article-title":"Kinetics of the reactions of nitrogen monoxide and nitrite with ferryl hemoglobin","volume":"34","author":"Herold","year":"2002","journal-title":"Free Rad. Biol. Med."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"14036","DOI":"10.1021\/bi0350349","article-title":"Metmyoglobin and methemoglobin catalyze the isomerization of peroxynitrite to nitrate","volume":"42","author":"Herold","year":"2003","journal-title":"Biochemistry"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"44049","DOI":"10.1074\/jbc.M305895200","article-title":"Reaction of human hemoglobin with peroxynitrite","volume":"278","author":"Romero","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_31","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_32","doi-asserted-by":"crossref","first-page":"12328","DOI":"10.1074\/jbc.272.19.12328","article-title":"Nitric oxide prevents oxidative damage produced by tert-butyl hydroperoxide in erythroleukemia cells via nitrosylation of heme and non-heme iron. Electron paramagnetic resonance evidence","volume":"272","author":"Gorbunov","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1089\/152308601300185160","article-title":"Antioxidant mechanisms of nitric oxide against iron-catalyzed oxidative stress in cells","volume":"3","author":"Kagan","year":"2001","journal-title":"Antioxid. Redox Signal."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1016\/S0006-2952(99)00007-6","article-title":"Tert-butyl hydroperoxide\/hemoglobin-induced oxidative stress and damage to vascular smooth muscle cells: Different effects of nitric oxide and nitrosothiols","volume":"57","author":"Shvedova","year":"1999","journal-title":"Biochem. Pharmacol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1134\/S0006350907030141","article-title":"Interaction between albumin-bound dinitrosyl iron complexes and reactive oxygen species","volume":"52","author":"Shumaev","year":"2007","journal-title":"Biophysics"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1042\/bj1710329","article-title":"Haemichrome formation from haemoglobin subunits by hydrogen peroxide","volume":"171","author":"Tomoda","year":"1978","journal-title":"Biochem. J."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/S0076-6879(08)36024-8","article-title":"Spectroscopic and crystallographic characterization of bis-histidyl adducts in tetrameric hemoglobins","volume":"436","author":"Vergara","year":"2008","journal-title":"Methods Enzymol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"30780","DOI":"10.1074\/jbc.M804709200","article-title":"Tyrosine residues as redox cofactors in human hemoglobin","volume":"283","author":"Reeder","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1021\/ar300234c","article-title":"Protein tyrosine nitration: Biochemical mechanisms and structural basis of its functional effects","volume":"46","author":"Radi","year":"2012","journal-title":"Acc. Chem. Res."},{"key":"ref_40","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_41","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."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"13493","DOI":"10.1021\/ja073349w","article-title":"Electron transfer between a tyrosyl radical and a cysteine residue in hemoproteins: Spin trapping analysis","volume":"129","author":"Bhattacharjee","year":"2007","journal-title":"J. Am. Chem. Soc."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"9908","DOI":"10.1016\/S0021-9258(18)48020-9","article-title":"Protein damage and degradation by oxygen radicals. III. Modification of secondary and tertiary structure","volume":"262","author":"Davies","year":"1987","journal-title":"J. Biol. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0300-483X(02)00191-9","article-title":"Nitric oxide trapping of the tyrosyl radical-chemistry and biochemistry","volume":"177","author":"Gunther","year":"2002","journal-title":"Toxicology"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"11304","DOI":"10.1021\/ja904832j","article-title":"Heme\/O2\/\u2022NO Nitric oxide dioxygenase (NOD) reactivity: Phenolic nitration via a putative heme-peroxynitrite intermediate","volume":"131","author":"Schopfer","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1042\/bj3210743","article-title":"One-electron oxidation pathway of peroxynitrite decomposition in human blood plasma: Evidence for the formation of protein tryptophan-centred radicals","volume":"321","author":"Pietraforte","year":"1997","journal-title":"Biochem. J."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1021\/tx950133b","article-title":"Peroxynitrite-dependent tryptophan nitration","volume":"9","author":"Alvarez","year":"1996","journal-title":"Chem. Res. Toxicol."},{"key":"ref_48","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_49","doi-asserted-by":"crossref","first-page":"40684","DOI":"10.1074\/jbc.M504503200","article-title":"Intramolecular electron transfer between tyrosyl radical and cysteine residue inhibits tyrosine nitration and induces thiyl radical formation in model peptides treated with myeloperoxidase, H2O2, and NO2\u2212: EPR spin-trapping studies","volume":"280","author":"Zhang","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"4894","DOI":"10.1074\/jbc.M609955200","article-title":"Structural Basis of Peroxide-mediated Changes in Human Hemoglobin","volume":"282","author":"Jia","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_51","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"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1038\/s41374-020-00492-3","article-title":"\u03b2Cysteine 93 in human hemoglobin: A gateway to oxidative stability in health and disease","volume":"101","author":"Alayash","year":"2021","journal-title":"Lab. Investig."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"13358","DOI":"10.1002\/chem.201100253","article-title":"Transformation of the {Fe(NO)2}9 dinitrosyl iron complexes (DNICs) into S-nitrosothiols (RSNOs) triggered by acid-base pairs","volume":"17","author":"Tsou","year":"2011","journal-title":"Chemistry"},{"key":"ref_54","unstructured":"Van Faassen, E., and Vanin, A.F. (2007). DNICs: Physico-Chemical Properties and Their Observation in Cells and Tissues. Radicals for Life: The Various Forms of Nitric Oxide, Elsevier."},{"key":"ref_55","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_56","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1039\/C8MT00048D","article-title":"The significance, trafficking and determination of labile iron in cytosol, mitochondria and lysosomes","volume":"10","author":"Lv","year":"2018","journal-title":"Metallomics"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"28926","DOI":"10.1074\/jbc.M707862200","article-title":"Nitric oxide induced conversion of cellular chelatable iron into macromolecular-bound paramagnetic diinitrosyliron complexes","volume":"283","author":"Toledo","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_58","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."},{"key":"ref_59","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 Biology"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"351.4","DOI":"10.1096\/fasebj.2019.33.1_supplement.351.4","article-title":"Can cellular labile iron pool be considered solely a pro-oxidant species in cells?","volume":"33","author":"Damasceno","year":"2019","journal-title":"FASEB J."},{"key":"ref_61","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"},{"key":"ref_62","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."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"3341","DOI":"10.1016\/S0021-9258(18)94071-8","article-title":"Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions","volume":"264","author":"Amici","year":"1989","journal-title":"J. Biol. Chem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/S0076-6879(96)69023-5","article-title":"Peroxynitrite dependent tyrosine nitration catalyzed by superoxide dismutase, myeloperoxidase and horseradish peroxidase","volume":"269","author":"Sampson","year":"1996","journal-title":"Methods Enzymol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1006\/abbi.2000.1699","article-title":"Rapid reactions of peroxynitrite with heme-thiolate proteins as the basis for protection of prostacyclin synthase from inactivation by nitration","volume":"376","author":"Zou","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"14085","DOI":"10.1074\/jbc.273.23.14085","article-title":"Inactivation of human manganese-superoxide dismutase by peroxynitrite is caused by exclusive nitration of tyrosine 34 to 3-nitrotyrosine","volume":"273","author":"Yamakura","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_67","first-page":"313","article-title":"A possible mechanism of the antioxidant action of dinitrosyl iron complexes","volume":"15","author":"Shumaev","year":"2021","journal-title":"Biochem. Suppl. Ser. B Biomed. Chem."},{"key":"ref_68","first-page":"137","article-title":"Nitric oxide-based protein modification: Formation and site-specificity of protein S-nitrosylation","volume":"4","author":"Kovacs","year":"2013","journal-title":"Front. Plant Sci."},{"key":"ref_69","doi-asserted-by":"crossref","unstructured":"Fernando, V., Zheng, X., Walia, Y., Sharma, V., Letson, J., and Furuta, S. (2019). S-Nitrosylation: An emerging paradigm of redox signaling. Antioxidants, 8.","DOI":"10.3390\/antiox8090404"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1331","DOI":"10.1089\/ars.2017.7403","article-title":"Protein S-nitrosylation: Determinants of specificity and enzymatic regulation of S-nitrosothiol-based signaling","volume":"30","author":"Stomberski","year":"2019","journal-title":"Antioxid. Redox Signal."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"4720","DOI":"10.1021\/ja512343w","article-title":"Nitric oxide is reduced to HNO by proton-coupled nucleophilic attack by ascorbate, tyrosine, and other alcohols. A new route to HNO in biological media?","volume":"137","author":"Suarez","year":"2015","journal-title":"J. Am. Chem. Soc."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1016\/j.niox.2012.11.001","article-title":"Dinitrosyl iron complexes with glutathione as NO and NO+ donors","volume":"29","author":"Borodulin","year":"2013","journal-title":"Nitric Oxide"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1134\/S0003683820050099","article-title":"Effect of iron\u2014Nitric oxide complexes on the reactivity of hemoglobin cysteines","volume":"56","author":"Kosmachevskaya","year":"2020","journal-title":"Appl. Biochem. Microbiol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/S0076-6879(94)33026-3","article-title":"Synthesis of peroxynitrite by a reaction of nitrite with acidified hydrogen peroxide in the presence of a quencher","volume":"233","author":"Beckman","year":"1994","journal-title":"Methods Enzymol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1403","DOI":"10.1021\/ac60178a039","article-title":"The determination of small concentrations of carbonyl groups in starch by the cyanohydrin method","volume":"33","author":"Schmorak","year":"1961","journal-title":"Anal. Chem."},{"key":"ref_76","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_77","doi-asserted-by":"crossref","first-page":"2096","DOI":"10.1039\/c3an36672c","article-title":"Quantification of protein thiols using ThioGlo1 fluorescent derivatives and HPLC separation","volume":"138","author":"Hoff","year":"2013","journal-title":"Analyst"},{"key":"ref_78","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"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/24\/13649\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T07:49:43Z","timestamp":1760168983000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/24\/13649"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,12,20]]},"references-count":78,"journal-issue":{"issue":"24","published-online":{"date-parts":[[2021,12]]}},"alternative-id":["ijms222413649"],"URL":"https:\/\/doi.org\/10.3390\/ijms222413649","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,12,20]]}}}