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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]
In the citing paper
“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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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
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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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