{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,20]],"date-time":"2026-08-20T16:02:34Z","timestamp":1787241754442,"version":"build-2736575974"},"reference-count":65,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2024,4,5]],"date-time":"2024-04-05T00:00:00Z","timestamp":1712275200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004569","name":"Ministry of Science and Higher Education","doi-asserted-by":"publisher","award":["N204077833"],"award-info":[{"award-number":["N204077833"]}],"id":[{"id":"10.13039\/501100004569","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Dinitrosyl iron complexes (DNICs) stabilize nitric oxide in cells and tissues and constitute an important form of its storage and transportation. DNICs may comprise low-molecular-weight ligands, e.g., thiols, imidazole groups in chemical compounds with low molecular weight (LMWDNICs), or high-molecular-weight ligands, e.g., peptides or proteins (HMWDNICs). The aim of this study was to investigate the role of low- and high-molecular-weight ligands in DNIC formation. Lysosomal and proteasomal proteolysis was inhibited by specific inhibitors. Experiments were conducted on human erythroid K562 cells and on K562 cells overexpressing a heavy chain of ferritin. Cell cultures were treated with \u2022NO donor. DNIC formation was monitored by electron paramagnetic resonance. Pretreatment of cells with proteolysis inhibitors diminished the intensity and changed the shape of the DNIC-specific EPR signal in a treatment time-dependent manner. The level of DNIC formation was significantly influenced by the presence of protein degradation products. Interestingly, formation of HMWDNICs depended on the availability of LMWDNICs. The extent of glutathione involvement in the in vivo formation of DNICs is minor yet noticeable, aligning with our prior research findings.<\/jats:p>","DOI":"10.3390\/molecules29071630","type":"journal-article","created":{"date-parts":[[2024,4,5]],"date-time":"2024-04-05T08:27:52Z","timestamp":1712305672000},"page":"1630","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["A Crucial Role of Proteolysis in the Formation of Intracellular Dinitrosyl Iron Complexes"],"prefix":"10.3390","volume":"29","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2707-2990","authenticated-orcid":false,"given":"Karolina E.","family":"W\u00f3jciuk","sequence":"first","affiliation":[{"name":"Nuclear Facilities Operations Department, National Centre for Nuclear Research (NCBJ), 05-400 Otwock, Poland"},{"name":"Centre for Radiobiology and Biological Dosimetry, Institute of Nuclear Chemistry and Technology, Dorodna 16, 03-195 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6758-7032","authenticated-orcid":false,"given":"Jaros\u0142aw","family":"Sad\u0142o","sequence":"additional","affiliation":[{"name":"Centre for Radiation Chemistry and Technology, Institute of Nuclear Chemistry and Technology, Dorodna 16, 03-195 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1960-1071","authenticated-orcid":false,"given":"Hanna","family":"Lewandowska","sequence":"additional","affiliation":[{"name":"Centre for Radiobiology and Biological Dosimetry, Institute of Nuclear Chemistry and Technology, Dorodna 16, 03-195 Warsaw, Poland"},{"name":"School of Health & Medical Sciences, University of Economics and Human Sciences in Warsaw, 59 Okopowa St., 01-043 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7310-5100","authenticated-orcid":false,"given":"Kamil","family":"Brz\u00f3ska","sequence":"additional","affiliation":[{"name":"Centre for Radiobiology and Biological Dosimetry, Institute of Nuclear Chemistry and Technology, Dorodna 16, 03-195 Warsaw, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4554-8566","authenticated-orcid":false,"given":"Marcin","family":"Kruszewski","sequence":"additional","affiliation":[{"name":"Centre for Radiobiology and Biological Dosimetry, Institute of Nuclear Chemistry and Technology, Dorodna 16, 03-195 Warsaw, Poland"},{"name":"Department of Molecular Biology and Translational Research, Institute of Rural Health, Jaczewskiego 2, 20-090 Lublin, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,4,5]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Lukiewicz, S., and Zweier, J.L. (1998). Nitric Oxide in Transplant Rejection and Anti-Tumor Defense, Kluwer Academic Publishers.","DOI":"10.1007\/978-1-4615-5081-5"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1254\/jjp.82.95","article-title":"The Physiological Activity and In Vivo Distribution of Dinitrosyl Dithiolato Iron Complex","volume":"82","author":"Ueno","year":"2000","journal-title":"Jpn. J. Pharmacol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"14682","DOI":"10.1021\/acs.chemrev.1c00253","article-title":"The Biologically Relevant Coordination Chemistry of Iron and Nitric Oxide: Electronic Structure and Reactivity","volume":"121","author":"Lehnert","year":"2021","journal-title":"Chem. Rev."},{"key":"ref_4","first-page":"99","article-title":"Mechanisms of Nitric Oxide Reactions Mediated by Biologically Relevant Metal Centers","volume":"154","author":"Ford","year":"2013","journal-title":"Nitrosyl Complexes Inorg. Chem. Biochem. Med. II"},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Vanin, A.F. (2021). Physico-Chemistry of Dinitrosyl Iron Complexes as a Determinant of Their Biological Activity. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms221910356"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1558","DOI":"10.1016\/j.freeradbiomed.2011.06.030","article-title":"Dinitrosyliron Complexes Are the Most Abundant Nitric Oxide-Derived Cellular Adduct: Biological Parameters of Assembly and Disappearance","volume":"51","author":"Hickok","year":"2011","journal-title":"Free Radic. Biol. Med."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1006\/niox.1997.0122","article-title":"Iron Catalyzes Both Decomposition and Synthesis ofS-Nitrosothiols: Optical and Electron Paramagnetic Resonance Studies","volume":"1","author":"Vanin","year":"1997","journal-title":"Nitric Oxide"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/j.redox.2017.12.007","article-title":"Differential Mitochondrial Dinitrosyliron Complex Formation by Nitrite and Nitric Oxide","volume":"15","author":"Thomas","year":"2018","journal-title":"Redox Biol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"2453","DOI":"10.1021\/acs.accounts.5b00246","article-title":"Synthetic Modeling Chemistry of Iron\u2013Sulfur Clusters in Nitric Oxide Signaling","volume":"48","author":"Fitzpatrick","year":"2015","journal-title":"Acc. Chem. Res."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"214171","DOI":"10.1016\/j.ccr.2021.214171","article-title":"Biological Iron-Sulfur Clusters: Mechanistic Insights from Mass Spectrometry","volume":"448","author":"Crack","year":"2021","journal-title":"Coord. Chem. Rev."},{"key":"ref_11","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_12","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1039\/B604194A","article-title":"Spectroscopic Characterization of Heme Iron\u2013Nitrosyl Species and Their Role in NO Reductase Mechanisms in Diiron Proteins","volume":"24","year":"2007","journal-title":"Nat. Prod. Rep."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"15831","DOI":"10.1021\/acs.inorgchem.1c03287","article-title":"Renaissance in NO Chemistry","volume":"60","author":"Ford","year":"2021","journal-title":"Inorg. Chem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"17695","DOI":"10.1002\/anie.201911968","article-title":"The Fe 2 (NO) 2 Diamond Core: A Unique Structural Motif In Non-Heme Iron-NO Chemistry","volume":"58","author":"Dong","year":"2019","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_15","unstructured":"Dong, H. (2021). Synthesis and Reactivity of Non-Heme Iron-Nitrosyl Complexes That Model the Active Sites of NO Reductases. [Ph.D. Thesis, University of Michigan]."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1134\/S0006350921040138","article-title":"Generation of Superoxide Radicals by Heart Mitochondria and the Effects of Dinitrosyl Iron Complexes and Ferritin","volume":"66","author":"Medvedeva","year":"2021","journal-title":"Biophysics"},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Mukosera, G.T., Principe, P., Mata-Greenwood, E., Liu, T., Schroeder, H., Parast, M., and Blood, A.B. (2022). Iron Nitrosyl Complexes Are Formed from Nitrite in the Human Placenta. J. Biol. Chem., 298.","DOI":"10.1016\/j.jbc.2022.102078"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1016\/j.freeradbiomed.2022.02.034","article-title":"Heme Oxygenase-Nitric Oxide Crosstalk-Mediated Iron Homeostasis in Plants under Oxidative Stress","volume":"182","author":"Singh","year":"2022","journal-title":"Free Radic. Biol. Med."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.ejphar.2014.07.017","article-title":"The Effect of Dinitrosyl Iron Complexes with Glutathione and S-Nitrosoglutathione on the Development of Experimental Endometriosis in Rats: A Comparative Studies","volume":"741","author":"Burgova","year":"2014","journal-title":"Eur. J. Pharmacol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1007\/s10103-020-03169-x","article-title":"Hypothetical Mechanism of Light Action on Nitric Oxide Physiological Effects","volume":"36","author":"Vladimir","year":"2021","journal-title":"Lasers Med. Sci."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/s00723-015-0744-6","article-title":"Dinitrosyl Iron Complexes with Persulfide Ligands: EPR and Optical Studies","volume":"47","author":"Vanin","year":"2016","journal-title":"Appl. Magn. Reson."},{"key":"ref_22","unstructured":"Vanin, A.F. (2019). Dinitrosyl Iron Complexes as a \u201cWorking Form\u201d of Nitric Oxide in Living Organisms, Cambridge Scholars Publishing."},{"key":"ref_23","unstructured":"Nalbandyan, R.M., Vanin, A.F., and Blumenfeld, L.A. EPR Signals of a New Type in Yeast Cells. Proceedings of the Abstracts of the Meeting Free Radical Processes in Biological Systems, Moscow, Russia."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1046\/j.1471-4159.2002.00864.x","article-title":"Impact of Endogenous Nitric Oxide on Microglial Cell Energy Metabolism and Labile Iron Pool","volume":"81","author":"Chenais","year":"2002","journal-title":"J. Neurochem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"3953","DOI":"10.1093\/jxb\/ern235","article-title":"Exposure to Nitric Oxide Protects against Oxidative Damage but Increases the Labile Iron Pool in Sorghum Embryonic Axes","volume":"59","author":"Jasid","year":"2008","journal-title":"J. Exp. Bot."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"12640","DOI":"10.1039\/C5DT00927H","article-title":"Formation of Glutathionyl Dinitrosyl Iron Complexes Protects against Iron Genotoxicity","volume":"44","author":"Lewandowska","year":"2015","journal-title":"Dalton Trans."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1002\/biof.1412","article-title":"LDL Dinitrosyl Iron Complex: A New Transferrin-independent Route for Iron Delivery in Hepatocytes","volume":"44","author":"Lewandowska","year":"2018","journal-title":"BioFactors"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"30980","DOI":"10.1074\/jbc.M101037200","article-title":"L-Cysteine-Mediated Destabilization of Dinitrosyl Iron Complexes in Proteins","volume":"276","author":"Rogers","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1016\/S1568-7864(03)00065-X","article-title":"Reversible Inactivation of E. Coli Endonuclease III via Modification of Its [4Fe-4S] Cluster by Nitric Oxide","volume":"2","author":"Rogers","year":"2003","journal-title":"DNA Repair"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"7964","DOI":"10.1021\/ja9030159","article-title":"Dinitrosyl Iron Complexes Relevant to Rieske Cluster Nitrosylation","volume":"131","author":"Tonzetich","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"6338","DOI":"10.1021\/ic9022757","article-title":"Detecting and Understanding the Roles of Nitric Oxide in Biology","volume":"49","author":"Tonzetich","year":"2010","journal-title":"Inorg. Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"15602","DOI":"10.1021\/ja8054996","article-title":"Reactions of Synthetic [2Fe-2S] and [4Fe-4S] Clusters with Nitric Oxide and Nitrosothiols","volume":"130","author":"Harrop","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"18168","DOI":"10.1021\/ja106290p","article-title":"Characterization of Iron Dinitrosyl Species Formed in the Reaction of Nitric Oxide with a Biological Rieske Center","volume":"132","author":"Tinberg","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"ref_34","first-page":"782","article-title":"Dinitrosyl Iron Complexes and S-Nitrosothiols Are Two Possible Forms for Stabilization and Transport of Nitric Oxide in Biological Systems","volume":"63","author":"Vanin","year":"1998","journal-title":"Biochem. c\/c Biokhimiia"},{"key":"ref_35","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":"Tung","year":"2021","journal-title":"Inorg. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1080\/10715769900301101","article-title":"In Vivo Distribution and Behavior of Paramagnetic Dinitrosyl Dithiolato Iron Complex in the Abdomen of Mouse","volume":"31","author":"Ueno","year":"1999","journal-title":"Free Radic. Res."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1016\/j.niox.2006.09.005","article-title":"Protein-Bound Dinitrosyl\u2013Iron Complexes Appearing in Blood of Rabbit Added with a Low-Molecular Dinitrosyl\u2013Iron Complex: EPR Studies","volume":"16","author":"Timoshin","year":"2007","journal-title":"Nitric Oxide"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1007\/s00775-006-0192-8","article-title":"Crucial Role of Lysosomal Iron in the Formation of Dinitrosyl Iron Complexes in vivo","volume":"12","author":"Lewandowska","year":"2007","journal-title":"J. Biol. Inorg. Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1002\/cyto.990190306","article-title":"Kinetic Analysis of Glutathione in Anchored Cells with Monochlorobimane","volume":"19","author":"Barhoumi","year":"1995","journal-title":"Cytometry"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1002\/biof.1418","article-title":"Dinitrosyl Iron Complexes: Formation and Antiradical Action in Heart Mitochondria","volume":"44","author":"Shumaev","year":"2018","journal-title":"BioFactors"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1006\/abbi.1996.0443","article-title":"Calpain Inhibitors and Serine Protease Inhibitors Can Produce Apoptosis in HL-60 Cells","volume":"334","author":"Lu","year":"1996","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1093\/carcin\/11.1.75","article-title":"Cysteine Proteinase Inhibitors and Ras. Gene Products Share the Same Biological Activities Including Tranforming Activity toward NIH3T3 Mouse Fibroblasts and the Differentiation-Inclucing Activity toward PC12 Rat Pheochromocytoma Cells","volume":"11","author":"Hiwasa","year":"1990","journal-title":"Carcinogenesis"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"752","DOI":"10.1002\/pro.5560050420","article-title":"Two Crystal Structures of the Leupeptin-Trypsin Complex","volume":"5","author":"Kurinov","year":"1996","journal-title":"Protein Sci."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1038\/aps.2013.5","article-title":"Application and Interpretation of Current Autophagy Inhibitors and Activators","volume":"34","author":"Yang","year":"2013","journal-title":"Acta Pharmacol. Sin."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1146\/annurev-physiol-012110-142317","article-title":"Lysosomal Acidification Mechanisms","volume":"74","author":"Mindell","year":"2012","journal-title":"Annu. Rev. Physiol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"13437","DOI":"10.1074\/jbc.272.20.13437","article-title":"Lactacystin and Clasto-Lactacystin \u03b2-Lactone Modify Multiple Proteasome \u03b2-Subunits and Inhibit Intracellular Protein Degradation and Major Histocompatibility Complex Class I Antigen Presentation","volume":"272","author":"Craiu","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1002\/jcp.1041590206","article-title":"Calpain Activation in Apoptosis","volume":"159","author":"Squier","year":"1994","journal-title":"J. Cell. Physiol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1083\/jcb.201210077","article-title":"Development of Proteasome Inhibitors as Research Tools and Cancer Drugs","volume":"199","author":"Goldberg","year":"2012","journal-title":"J. Cell Biol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1042\/bj20030282","article-title":"Changes in the Proteolytic Activities of Proteasomes and Lysosomes in Human Fibroblasts Produced by Serum Withdrawal, Amino-Acid Deprivation and Confluent Conditions","volume":"375","author":"Fuertes","year":"2003","journal-title":"Biochem. J."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/S0962-8924(98)01346-4","article-title":"Proteasome Inhibitors: Valuable New Tools for Cell Biologists","volume":"8","author":"Lee","year":"1998","journal-title":"Trends Cell Biol."},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Kageyama, M., Ota, T., Sasaoka, M., Katsuta, O., and Shinomiya, K. (2019). Chemical Proteasome Inhibition as a Novel Animal Model of Inner Retinal Degeneration in Rats. PLoS ONE, 14.","DOI":"10.1371\/journal.pone.0217945"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1002\/ijc.24004","article-title":"Induction of the Lysosomal Apoptosis Pathway by Inhibitors of the Ubiquitin-proteasome System","volume":"124","author":"Berndtsson","year":"2009","journal-title":"Int. J. Cancer"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"8264","DOI":"10.1021\/bi060542e","article-title":"Identification of the Proteasome Inhibitor MG262 as a Potent ATP-Dependent Inhibitor of the Salmonella Enterica Serovar Typhimurium Lon Protease","volume":"45","author":"Frase","year":"2006","journal-title":"Biochemistry"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1124\/jpet.111.190710","article-title":"Proteasome Inhibition Reduces Proliferation, Collagen Expression, and Inflammatory Cytokine Production in Nasal Mucosa and Polyp Fibroblasts","volume":"343","author":"Pujols","year":"2012","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/0968-0004(91)90058-4","article-title":"Cell-Penetrating Inhibitors of Calpain","volume":"16","author":"Mehdi","year":"1991","journal-title":"Trends Biochem. Sci."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1124","DOI":"10.1016\/S1359-6446(02)02402-9","article-title":"Proteinase and Peptidase Inhibition: Recent Potential Targets for Drug Development","volume":"7","author":"Barrett","year":"2002","journal-title":"Drug Discov. Today"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1006\/niox.1998.0180","article-title":"The 2.03 Signal as an Indicator of Dinitrosyl-Iron Complexes with Thiol-Containing Ligands","volume":"2","author":"Vanin","year":"1998","journal-title":"Nitric Oxide"},{"key":"ref_59","unstructured":"Lipinski, P., Lewandowska, H., Drapier, J.C., Starzynski, R.R., Bartlomiejczyk, T., and Kruszewski, M. (2003). Increase in Labile Iron Pool (LIP) Level and Generation of EPR-Detectable Dinitrosyl-Non-Heme Iron Complexes in L5178Y Cells Exposed to Nitric Oxide. Possible Role of LIP as a Source of Iron for DNIC Formation, Deregulations du Metabolisme du fer. Chimie, biologie et therapeutiques."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"3679","DOI":"10.1021\/bi00178a026","article-title":"Identification of the EPR-Active Iron-Nitrosyl Complexes in Mammalian Ferritins","volume":"33","author":"Lee","year":"1994","journal-title":"Biochemistry"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"6732","DOI":"10.1016\/j.bmc.2012.09.032","article-title":"Coordination of Iron Ions in The Form of Histidinyl Dinitrosyl Complexes Does Not Prevent Their Genotoxicity","volume":"20","author":"Lewandowska","year":"2012","journal-title":"Bioorganic Med. Chem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"42172","DOI":"10.1074\/jbc.M507916200","article-title":"Nitrosylation of Human Glutathione Transferase P1-1 with Dinitrosyl Diglutathionyl Iron Complex in vitro and in vivo","volume":"280","author":"Cesareo","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"42283","DOI":"10.1074\/jbc.M305568200","article-title":"The Specific Interaction of Dinitrosyl-Diglutathionyl-Iron Complex, a Natural NO Carrier, with the Glutathione Transferase Superfamily: Suggestion for an Evolutionary Pressure in the Direction of the Storage of Nitric Oxide","volume":"278","author":"Pedersen","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_64","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_65","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.niox.2005.09.005","article-title":"Imidazole Derivatives as Antioxidants and Selective Inhibitors of nNOS","volume":"14","author":"Sorrenti","year":"2006","journal-title":"Nitric Oxide"}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/29\/7\/1630\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T14:23:48Z","timestamp":1760106228000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/29\/7\/1630"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,4,5]]},"references-count":65,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2024,4]]}},"alternative-id":["molecules29071630"],"URL":"https:\/\/doi.org\/10.3390\/molecules29071630","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,4,5]]}}}