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Dinitrosyl iron complexes with thiolate ligands: Physico-chemistry, biochemistry and physiology
Abstract
Some present-day concepts on the origin and functional activities of dinitrosyl iron complexes (DNIC) with thiolate ligands are considered. Nitric oxide (NO) including to DNIC increases its stability and ensures effective targeting of NO to organs and tissues. DNIC have a square-planar structure; unpaired electron is localized on the d(z2) orbital of the d(7) iron atom. The formula of DNIC appears as [(RS(-))(2)Fe(+)(NO(+))(2)....((-)SR)(2)](-); electron spin is S=1/2. Conversion of an originally diamagnetic group, Fe(2+)(NO)(2) with electron configuration d(8), into a paramagnetic Fe(+)(NO(+))(2) group is a result of disproportionation of NO ligands and substitution of newly generated NO(-) for NO. The nitrosonium ions present in DNIC impart to them high nitrosylating activity, e.g., ability to induce S-nitrosylation of thiols. The ability of S-nitrosothiols to form DNIC in a direct reaction with bivalent iron is a prerequisite to effective mutual conversions of DNIC and S-nitrosothiols. In this work, I consider some mechanisms of destructive effects of low-molecular DNIC on active centers of iron-sulfur proteins, ability of DNIC to express certain genes, to activate guanylate cyclase, to exert hypotensive, vasodilator effects, to inhibit platelet aggregation, to accelerate wound healing and to produce potent erective action. Recently a stabilized powder-like polymeric composition based on dimeric glutathione DNIC the water-soluble polymer in which was used as a filling agent was designed. The advantages of this stable DNIC-glutathione preparation include their ability to retain their physico-chemical and functional activities within at least one year. At present, the preparation undergo testing as a base for the design of a wide variety of broad-spectrum drugs.
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“It was proposed that DNICs are formed in the vasculature from nitrosothiols and that they are in equilibrium with the nitrosothiol pool [103,104].”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [103]
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Cites
Castagna, M., Takai, Y., Kaibuchi, K., Sano, K., Kikkawa, U., & Nishizuka, Y. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34459-4 · Cited by 4,725
(1992) · doi:10.1126/science.1378650 · Cited by 1,163
Guanylate cyclase and the ⋅NO/cGMP signaling pathway
Denninger, J. W., & Marletta, M. A. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00024-9 · Cited by 1,040
Rajfer, J., Aronson, W. J., Bush, P. A., Dorey, F. J., & Ignarro, L. J. (1992) · New England Journal of Medicine · doi:10.1056/nejm199201093260203 · Cited by 1,006
Methods in Nitric Oxide Research
Young, J. (1997) · Physiological Measurement · doi:10.1088/0967-3334/18/1/008 · Cited by 749
The emerging biology of the nitrite anion
Gladwin, M. T., Schechter, A. N., Kim-Shapiro, D. B., Patel, R. P., Hogg, N., Shiva, S., Cannon, R. O., Kelm, M., Wink, D. A., Espey, M. G., et al. (2005) · Nature Chemical Biology · doi:10.1038/nchembio1105-308 · Cited by 609
Nitric oxide and the regulation of gene expression
Bogdan, C. (2001) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01900-0 · Cited by 534
EPR demonstration of iron-nitrosyl complex formation by cytotoxic activated macrophages
Lancaster, J. R., & Hibbs, J. B. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.3.1223 · Cited by 507
Shafirovich, V., & Lymar, S. V. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.112202099 · Cited by 441
Nitrosation and oxidation in the regulation of gene expression
Marshall, H. E., Merchant, K., & Stamler, J. S. (2000) · The FASEB Journal · doi:10.1096/fj.00.011rev · Cited by 421
Research works printed but not linked: 19
- Vanin, 1967, Investigation of non-heme iron complexes in cells and tissues by the EPR method, Biofizika (Rus), 12, 829
- Vanin, 1967, Identification of divalent iron complexes with cysteine in biological systems, Biokhimiya (Rus), 32, 228
- A.F. Vanin, L.A. Blumenfeld, D.Sh. Burbaev, I.L. Lisovskaya, A.G. Chetverikov, Investigations of some iron complexes in biological objects, Proceedings of the International Jubilee Conference on Paramagnetic Resonance, 1969 June 15–20, Kazan, Part 1 (1970) 218–223.
- Vanin, 1971, Endogenous heme and non-heme nitrosyl iron complexes in cells and tissues, Biofizika (Rus), 16, 650
- Mikoyan, 2004, Formation of paramagnetic nitrosyl complexes of nonheme iron in the animal organism with the participation of nitric oxide from exogenous and endogenous sources, Biophysics (Translation from Russian), 41, 110
- Vanin, 1992, Dinitrosyl-iron complexes with thiol-containing ligands and their reversible transformation into nitrosothiols, Biokhimiya (Rus), 58, 1103
- A.F. Vanin, Nitrosyl non-heme iron complexes in animal tissues and microorganisms, D.Sc.Thesis, Institute of Chemical Physics, Moscow, 1980.
- Burbaev, 1971, Electronic and spatial structures of paramagnetic dinitrosyl ferrous complexes, Zhurnal Strukt. Khimii (Rus), 2, 252
- Sanina, 2004, Structure of neutral mononuclear dinitrosyl iron complex with 1,2,4-triazole-3-thione [Fe(SC3H3N3)2(NO)2]0.5H2O, Mendeleev Communs., 1, 1
- Vanin, 1975, On the origin of paramagnetic centers at g=2.03 in animal tissues and microorganisms, Studia Biofizika, 49, 13
- Vanin, 1980, On the mechanism of nitrosyl non-heme iron formation in animal tissue, Studia Biofizika, 80, 221
- Voevodskaya, 1999, The nitric oxide-mediated degradation of active center in an iron-sulphur protein adrenodoxin, Current Top. Biophys., 23, 31
- Kleschyov, 1985, Role of nitric oxide and iron in hypotensive action of nitrosyl iron complexes with various anionic ligands, Studia Biofizika, 105, 93
- Mordvintcev, 1988, Hypotensive activity of dinitrosyl complexes of iron in narcotized animals, Bulleten Vsesoyuznogo Kardiol. Nauchnogo Tsentra SSSR, 1, 46
- Galagan, 1988, Hypotensive effect of dinitrosyl complexes of iron in conscious animals, Bulleten Vsesoyuznogo Kardiol. Nauchnogo Centra SSSR, 2, 75
- Van der Viet, 1998, Formation of S-nitrosothiols via direct nucleophylic nitrosation of thiols by peroxynitrite with elimination of hydrogen peroxide, J. Biol. Chem., 273, 30225
- Mordvintcev, 1986, The inhibitory effect of low-molecular dinitrosyl iron complexes on platelet aggregation, Biokhimiya (Rus), 51, 1851
- Kuznetsov, 1988, Low-molecular and protein-bound dinitrosyl iron complexes as inhibitors of platelet aggregation, Voprosy Med. Khimii, 5, 43
- Kurbanov, 1989, Effects of thiol-containing compounds and iron on the formation of nitric oxide from nitroprusside and nitroglycerine, Voprosy Med Khimii (Rus), 6, 87
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Metadata
- Authors
- Vanin, A. F.
- Affiliations
- Russian Academy of Sciences (RU)
- Corresponding author
- Vanin, Anatoly F.
- ORCID
- Vanin, Anatoly F.
- Venue
- Nitric Oxide
- Publisher
- Elsevier BV
- Published
- 2009-08
- Volume
- 21
- Issue
- 1
- Pages
- 1-13
- ISSN
- 1089-8603 (ISSN-L)
- OpenAlex
- W2044091187
- Cited by
- 217
- References
- 126
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 2 · 2023: 9 · 2022: 10 · 2021: 11 · 2020: 12 · 2019: 9 · 2018: 15 · 2017: 15 · 2016: 13 · 2015: 16 · 2014: 28 · 2013: 21 · 2012: 19
- FWCI
- 1.87
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nitric Oxide (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Russian Foundation for Basic Research
- Topics
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- dinitrosyl iron complexes, thiolate ligands, nitrosonium ion, S-nitrosylation, S-nitrosothiols, iron-sulfur proteins, guanylate cyclase activation, platelet aggregation inhibition, wound healing, erectile function, glutathione, polymeric drug delivery
- MeSH terms
- Animals, Electron Spin Resonance Spectroscopy, Iron, Liver, Nitric Oxide, Nitrogen Oxides, Sulfhydryl Compounds, Chemical Phenomena
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