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Dinitrosyliron complexes are the most abundant nitric oxide-derived cellular adduct: biological parameters of assembly and disappearance
Open accessAbstract
It is well established that nitric oxide ((•)NO) reacts with cellular iron and thiols to form dinitrosyliron complexes (DNIC). Little is known, however, regarding their formation and biological fate. Our quantitative measurements reveal that cellular concentrations of DNIC are proportionally the largest of all (•)NO-derived adducts (900 pmol/mg protein, or 45-90 μM). Using murine macrophages (RAW 264.7), we measured the amounts, and kinetics, of DNIC assembly and disappearance from endogenous and exogenous sources of (•)NO in relation to iron and O(2) concentration. Amounts of DNIC were equal to or greater than measured amounts of chelatable iron and depended on the dose and duration of (•)NO exposure. DNIC formation paralleled the upregulation of iNOS and occurred at low physiologic (•)NO concentrations (50-500 nM). Decreasing the O(2) concentration reduced the rate of enzymatic (•)NO synthesis without affecting the amount of DNIC formed. Temporal measurements revealed that DNIC disappeared in an oxygen-independent manner (t(1/2)=80 min) and remained detectable long after the (•)NO source was removed (>24 h). These results demonstrate that DNIC will be formed under all cellular settings of (•)NO production and that the contribution of DNIC to the multitude of observed effects of (•)NO must always be considered.
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“Reaction of excess NO with the CIP leads to quantitative conversion to paramagnetic dinitrosyliron complexes (DNICs) with thiol containing ligands [250, 251].”
From Signaling and stress: The redox landscape in NOS2 biology (2015) · cites this paper as [250]
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“Thomas et al. proposed these species to represent the most abundant NOcontaining material in biological tissue [102].”
From On the chemical biology of the nitrite/sulfide interaction (2015) · cites this paper as [102]
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Cites
Ahmed, S., Gogal, R., & Walsh, J. (1994) · JIM - Journal of Immunological Methods · doi:10.1016/0022-1759(94)90396-4 · Cited by 1,450
The chemical biology of nitric oxide: Implications in cellular signaling
Thomas, D. D., Ridnour, L. A., Isenberg, J. S., Flores-Santana, W., Switzer, C. H., Donzelli, S., Hussain, P., Vecoli, C., Paolocci, N., Ambs, S., et al. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.03.020 · Cited by 975
Self-citationThe biological lifetime of nitric oxide: Implications for the perivascular dynamics of NO and O 2
Thomas, D. D., Liu, X., Kantrow, S. P., & Lancaster, J. R. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.1.355 · Cited by 760
Self-citationNitric oxide as a unique signaling molecule in the vascular system: a historical overview.
Ignarro, L. J. (2002) · PubMed · Cited by 635
Melillo, G., Musso, T., Sica, A., Taylor, L. S., Cox, G. W., & Varesio, L. (1995) · The Journal of Experimental Medicine · doi:10.1084/jem.182.6.1683 · Cited by 625
A Tutorial on the Diffusibility and Reactivity of Free Nitric Oxide
Lancaster, J. R. (1997) · Nitric Oxide · doi:10.1006/niox.1996.0112 · Cited by 495
Drapier, J., Pellat‐Deceunynck, C., & Henry, Y. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99204-5 · Cited by 279
S-nitrosation of serum albumin by dinitrosyl-iron complex
Boese, M., Mordvintcev, P. I., Vanin, A. F., Busse, R., & Mülsch, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.49.29244 · Cited by 259
Measurement of circulating nitrite and S-nitrosothiols by reductive chemiluminescence
MacArthur, P. H., Shiva, S., & Gladwin, M. T. (2007) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.12.012 · Cited by 235
The Chelatable Iron Pool in Living Cells: A Methodically Defined Quantity
Petrat, F. M., de GROOT, H., Sustmann, R., & Rauen, U. (2002) · Biological Chemistry · doi:10.1515/bc.2002.051 · Cited by 234
Bosworth, C. A., Toledo, J. C., Zmijewski, J. W., Li, Q., & Lancaster, J. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710416106 · Cited by 220
Dinitrosyl iron complexes with thiolate ligands: physico-chemistry, biochemistry and physiology
Vanin, A. F. (2009) · Nitric Oxide · doi:10.1016/j.niox.2009.03.005 · Cited by 217
Baker, P. R. S., Schopfer, F. J., Sweeney, S., & Freeman, B. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402587101 · Cited by 201
Albakri, Q., & Stuehr, D. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.10.5414 · Cited by 178
Changes in Electron Spin Resonance Signals of Rat Liver During Chemical Carcinogenesis
Vithayathil, A. J., Ternberg, J. L., & Commoner, B. (1965) · Nature · doi:10.1038/2071246a0 · Cited by 156
Watts, R., Hawkins, C. L., Ponka, P., & Richardson, D. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602515103 · Cited by 128
The 2.03 Signal as an Indicator of Dinitrosyl–Iron Complexes with Thiol-Containing Ligands
Vanin, A. F., Сереженков, В. А., Mikoyan, V. D., & Mv, G. (1998) · Nitric Oxide · doi:10.1006/niox.1998.0180 · Cited by 125
Toledo, J. C., Bosworth, C. A., Hennon, S. W., Mahtani, H., Bergonia, H. A., & Lancaster, J. R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707862200 · Cited by 119
Melillo, G., Taylor, L. S., Brooks, A., Cox, G. W., & Varesio, L. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.157.6.2638 · Cited by 104
Quantitation of intracellular free iron by electron paramagnetic resonance spectroscopy
Woodmansee, A. N., & Imlay, J. A. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)49316-0 · Cited by 99
Radicals for life : the various forms of nitric oxide
van Faassen, E., & Vanin, A. F. (2007) · Elsevier eBooks · Cited by 92
Vanin, A. F., Stukan, R. A., & Manukhina, E. B. (1996) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(95)00247-2 · Cited by 92
Thomas, D. D., Miranda, K. M., Graham Espey, M., Citrin, D., Jourd'heuil, D., Paolocci, N., Hewett, S. J., Colton, C. A., Grisham, M. B., Feelisch, M., et al. (2002) · Methods in Enzymology · doi:10.1016/s0076-6879(02)59174-6 · Cited by 76
Self-citationSeverina, I. S., Busygina, O. G., Pyatakova, N. V., Malenkova, I. V., & Vanin, A. F. (2003) · Nitric Oxide · doi:10.1016/s1089-8603(03)00002-8 · Cited by 73
Mallard, J. R., & Kent, M. N. (1964) · Nature · doi:10.1038/2041192a0 · Cited by 64
Turella, P., Pedersen, J. Z., Caccuri, A. M., Maria, F. D., Mastroberardino, P. G., Bello, M. L., Federici, G., & Ricci, G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305569200 · Cited by 64
[FREE RADICALS OF A NEW TYPE IN YEAST CELLS].
Vanin, A. F., & Rm, N. (1965) · PubMed · Cited by 62
Dinitrosyl–iron complexes with thiol-containing ligands: Spatial and electronic structures
Vanin, A. F., Санина, Н. А., Сереженков, В. А., Burbaev, D. S., Lozinsky, V. I., & Aldoshin, S. M. (2006) · Nitric Oxide · doi:10.1016/j.niox.2006.07.005 · Cited by 58
Inactivation of Soluble Guanylate Cyclase by Stoichiometric S-Nitrosation
Mayer, B., Kleschyov, A. L., Stessel, H., Russwurm, M., Münzel, T. F., Koesling, D., & Schmidt, K. (2008) · Molecular Pharmacology · doi:10.1124/mol.108.052142 · Cited by 55
Mokh, V. P., Poltorakov, А. P., Сереженков, В. А., & Vanin, A. F. (2010) · Nitric Oxide · doi:10.1016/j.niox.2010.01.002 · Cited by 31
Physiological and hypoxic O2 tensions rapidly regulate NO production by stimulated macrophages
Robinson, M. A., Baumgardner, J. E., Good, V. P., & Otto, C. M. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00469.2007 · Cited by 28
[Hypotensive effect of dinitrosyl iron complexes in experiments on waking animals].
Galagan, M. E., Oranovskaia, E. V., Mordvintsev, P. I., Os, M., & Vanin, A. F. (1988) · PubMed · Cited by 9
[Hypotensive activity of the nitrosyl complexes of nonheme iron with different anionic ligands].
Vanin, A. F., Kleshchev, A. L., Mordvintsev, P. I., & Kr, S. (1985) · PubMed · Cited by 6
[Dinitrosyl complexes of nonheme iron in the blood plasma of animals and man].
Ni, M., & Vanin, A. F. (1989) · PubMed · Cited by 1
Cited by
Sorted by citations
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Toledo, J. C., & Augusto, O. (2012) · Chemical Research in Toxicology · doi:10.1021/tx300042g · Cited by 294
Lehnert, N., Kim, E., Dong, H. T., Harland, J. B., Hunt, A. P., Manickas, E. C., Oakley, K. M., Pham, J., Reed, G. C., & Alfaro, V. S. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00253 · Cited by 283
Thomas, D. D. (2015) · Redox Biology · doi:10.1016/j.redox.2015.05.002 · Cited by 179
Self-citationSignaling and stress: The redox landscape in NOS2 biology
Thomas, D. D., Heinecke, J. L., Ridnour, L. A., Cheng, R. Y., Kesarwala, A. H., Switzer, C. H., McVicar, D. W., Roberts, D. D., Glynn, S., Fukuto, J. M., et al. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.06.002 · Cited by 150
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Ma, L., Azad, M. G., Dharmasivam, M., Richardson, V., Quinn, R. J., Feng, Y., Pountney, D. L., Tonissen, K. F., Mellick, G. D., Yanatori, I., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101896 · Cited by 151
Metadata
- Authors
- Hickok, J. R., Sahni, S., Shen, H., Arvind, A., Antoniou, C., Fung, L. W. M., & Thomas, D. D.
- Affiliations
- University of Illinois Chicago (US)
- University of Chicago (US)
- Corresponding author
- Thomas, Douglas D.
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2011-10
- Volume
- 51
- Issue
- 8
- Pages
- 1558-1566
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC3172375
- OpenAlex
- W2085719171
- Cited by
- 155
- References
- 34
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 9 · 2023: 10 · 2022: 6 · 2021: 16 · 2020: 11 · 2019: 13 · 2018: 13 · 2017: 12 · 2016: 14 · 2015: 7 · 2014: 14 · 2013: 9 · 2012: 8
- FWCI
- 7.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (K22CA113315)
- National Institute of General Medical Sciences (R01GM068621, R01GM094175)
- Topics
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- nitric oxide, iron, thiols, macrophages, inducible nitric oxide synthase, oxygen concentration
- MeSH terms
- Animals, Cell Line, Electron Spin Resonance Spectroscopy, Iron, Macrophages, Nitric Oxide, Nitrogen Oxides, Oxygen, Reactive Nitrogen Species, Mice
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