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.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Excess NO reacts with the chelatable iron pool to quantitatively convert it to paramagnetic DNICs with thiol ligands.
“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]
Thomas et al. proposed that dinitrosyl-iron-complexes (DNICs) represent the most abundant NO-containing material in biological tissue.
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
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 · see citing works
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 · see citing works
Self-citationThomas, 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 · see citing works
Self-citationMelillo, 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 626 · see citing works
Nitric oxide as a unique signaling molecule in the vascular system: a historical overview.
Ignarro, L. J. (2002) · PubMed · Cited by 623 · see citing works
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 · see citing works
Drapier, J., Pellat‐Deceunynck, C., & Henry, Y. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99204-5 · Cited by 279 · see citing works
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 · see citing works
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 230 · see citing works
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 229 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Albakri, Q., & Stuehr, D. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.10.5414 · Cited by 182 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 117 · see citing works
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 · see citing works
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 · see citing works
Radicals for life : the various forms of nitric oxide
van Faassen, E., & Vanin, A. F. (2007) · Elsevier eBooks · Cited by 92 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Mallard, J. R., & Kent, M. N. (1964) · Nature · doi:10.1038/2041192a0 · Cited by 64 · see citing works
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 · see citing works
[FREE RADICALS OF A NEW TYPE IN YEAST CELLS].
Vanin, A. F., & Rm, N. (1965) · PubMed · Cited by 62 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
[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 · see citing works
[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 · see citing works
[Dinitrosyl complexes of nonheme iron in the blood plasma of animals and man].
Ni, M., & Vanin, A. F. (1989) · PubMed · Cited by 1 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Connecting the Chemical and Biological Properties of Nitric Oxide
Toledo, J. C., & Augusto, O. (2012) · Chemical Research in Toxicology · doi:10.1021/tx300042g · Cited by 285 · see citing works
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 277 · see citing works
Thomas, D. D. (2015) · Redox Biology · doi:10.1016/j.redox.2015.05.002 · Cited by 168 · see citing works
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 · see citing works
Self-citationParkinson's disease: Alterations in iron and redox biology as a key to unlock therapeutic strategies
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 148 · see citing works
Fang, B., Kovačević, Ž., Park, K. C., Kalinowski, D. S., Jansson, P. J., Lane, D. J. R., Sahni, S., & Richardson, D. R. (2013) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2013.11.002 · Cited by 148 · see citing works
Self-citationGlutathione, Glutaredoxins, and Iron
Berndt, C., & Lillig, C. H. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7132 · Cited by 141 · see citing works
Specificity in S-Nitrosylation: A Short-Range Mechanism for NO Signaling?
Martı́nez-Ruiz, A., Araújo, I. M., Izquierdo-Álvarez, A., Hernansanz‐Agustín, P., Lamas, S., & Serrador, J. M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5066 · Cited by 121 · see citing works
Hickok, J. R., Vasudevan, D., Antholine, W. E., & Thomas, D. D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.432294 · Cited by 120 · see citing works
Self-citationOn the chemical biology of the nitrite/sulfide interaction
Cortese-Krott, M. M., Fernandez, B. O., Kelm, M., Butler, A. R., & Feelisch, M. (2015) · Nitric Oxide · doi:10.1016/j.niox.2014.12.009 · Cited by 115 · see citing works
Vanin, A. F. (2016) · Nitric Oxide · doi:10.1016/j.niox.2016.01.006 · Cited by 113 · see citing works
Nitric Oxide Signaling and Regulation in the Cardiovascular System: Recent Advances
Carlström, M., Weitzberg, E., & Lundberg, J. O. (2024) · Pharmacological Reviews · doi:10.1124/pharmrev.124.001060 · Cited by 103 · see citing works
The solution chemistry of nitric oxide and other reactive nitrogen species
Ford, P. C., & Miranda, K. M. (2020) · Nitric Oxide · doi:10.1016/j.niox.2020.07.004 · Cited by 100 · see citing works
Hickok, J. R., Sahni, S., Mikhed, Y., Bonini, M. G., & Thomas, D. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.287052 · Cited by 80 · see citing works
Self-citationEpigenetics: The third pillar of nitric oxide signaling
Socco, S., Bovee, R. C., Palczewski, M. B., Hickok, J. R., & Thomas, D. D. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.04.011 · Cited by 80 · see citing works
Self-citationNitric oxide imaging in cancer enabled by steric relaxation of a photoacoustic probe platform
Reinhardt, C. J., Xu, R., & Chan, J. (2020) · Chemical Science · doi:10.1039/c9sc05600a · Cited by 77 · see citing works
Nitric oxide and the thioredoxin system: a complex interplay in redox regulation
Benhar, M. (2015) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2015.09.010 · Cited by 75 · see citing works
Nitrosothiol formation and S-nitrosation signaling through nitric oxide synthases
Wynia‐Smith, S. L., & Smith, B. C. (2016) · Nitric Oxide · doi:10.1016/j.niox.2016.10.001 · Cited by 73 · see citing works
Farahani, A., Farahani, A., Kashfi, K., & Ghasemi, A. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.107781 · Cited by 76 · see citing works
Narne, P., Pandey, V., & Phanithi, P. B. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1141-6 · Cited by 70 · see citing works
Lu, T., Wang, Y., Hung, C., Chiou, S.-J., & Liaw, W. (2018) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.8b01818 · Cited by 68 · see citing works
Rahmanto, Y. S., Kalinowski, D. S., Lane, D. J. R., Lok, H. C., Richardson, V., & Richardson, D. R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.329847 · Cited by 66 · see citing works
Speelman, A. L., Zhang, B., Silakov, A., Skodje, K. M., Alp, E. E., Zhao, J. Y., Hu, M. Y., Kim, E., Krebs, C., & Lehnert, N. (2016) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.6b00510 · Cited by 66 · see citing works
Catalase (KatA) Plays a Role in Protection against Anaerobic Nitric Oxide in Pseudomonas aeruginosa
Su, S., Panmanee, W., Wilson, J. J., Mahtani, H. K., Li, Q., VanderWielen, B. D., Makris, T. M., Rogers, M., McDaniel, C. T., Lipscomb, J. D., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0091813 · Cited by 62 · see citing works
Nitric oxide, the new architect of epigenetic landscapes
Vasudevan, D., Bovee, R. C., & Thomas, D. D. (2016) · Nitric Oxide · doi:10.1016/j.niox.2016.08.002 · Cited by 63 · see citing works
Self-citationKeszler, Á., Lindemer, B. J., Hogg, N., Weihrauch, D., & Lohr, N. L. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.05.006 · Cited by 59 · see citing works
Lok, H. C., Rahmanto, Y. S., Hawkins, C. L., Kalinowski, D. S., Morrow, C. S., Townsend, A. J., Ponka, P., & Richardson, D. R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.310987 · Cited by 57 · see citing works
Synthetic Advances Inspired by the Bioactive Dinitrosyl Iron Unit
Pulukkody, R., & Darensbourg, M. Y. (2015) · Accounts of Chemical Research · doi:10.1021/acs.accounts.5b00215 · Cited by 54 · see citing works
Al-Akra, L., Bae, D.-H., Sahni, S., Huang, M. L. H., Park, K. C., Lane, D. J. R., Jansson, P. J., & Richardson, D. R. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.772699 · Cited by 54 · see citing works
Self-citationIron sulfur cluster proteins and microbial regulation: implications for understanding tuberculosis
Saini, V., Farhana, A., Glasgow, J. N., & Steyn, A. J. C. (2012) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2012.03.004 · Cited by 53 · see citing works
Li, Q., Li, C., Mahtani, H. K., Du, J., Patel, A. R., & Lancaster, J. R. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.569764 · Cited by 52 · see citing works
Physico-Chemistry of Dinitrosyl Iron Complexes as a Determinant of Their Biological Activity
Vanin, A. F. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910356 · Cited by 52 · see citing works
Pereira, J. C. M., Iretskii, A. V., Han, R., & Ford, P. C. (2014) · Journal of the American Chemical Society · doi:10.1021/ja510393q · Cited by 51 · see citing works
Kwon, Y. M., Delgado, M., Zakharov, L. N., Seda, T., & Gilbertson, J. D. (2016) · Chemical Communications · doi:10.1039/c6cc05962g · Cited by 53 · see citing works
Dinitrosyl Iron Complexes (DNICs). From Spontaneous Assembly to Biological Roles
Truzzi, D. R., Medeiros, N. M., Augusto, O., & Ford, P. C. (2021) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.1c00823 · Cited by 51 · see citing works
Anand, K., Tripathi, A. P., Shukla, K., Malhotra, N., Jamithireddy, A. K., Jha, R., Chaudhury, S., Rajmani, R. S., Ramesh, A., Nagaraja, V., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102062 · Cited by 45 · see citing works
Oxygen dependence of nitric oxide-mediated signaling
Hickok, J. R., Vasudevan, D., Jablonski, K., & Thomas, D. D. (2013) · Redox Biology · doi:10.1016/j.redox.2012.11.002 · Cited by 47 · see citing works
Self-citationAmbidentate Thiocyanate and Cyanate Ligands in Dinitrosyl Iron Complexes
Hsieh, C., Brothers, S. M., Reibenspies, J. H., Hall, M. B., Popescu, C. V., & Darensbourg, M. Y. (2013) · Inorganic Chemistry · doi:10.1021/ic3025149 · Cited by 47 · see citing works
Cortes, T., Schubert, O. T., Banaei‐Esfahani, A., Collins, B. C., Aebersold, R. H., & Young, D. (2017) · Scientific Reports · doi:10.1038/s41598-017-08306-1 · Cited by 45 · see citing works
Vanin, A. F. (2019) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-019-00886-1 · Cited by 45 · see citing works
Russell, T. M., & Richardson, D. R. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102568 · Cited by 43 · see citing works
Monteiro, H. P., Ogata, F. T., & Stern, A. (2017) · Biomedical Journal · doi:10.1016/j.bj.2017.06.002 · Cited by 45 · see citing works
Nitric oxide reduces oxidative stress in cancer cells by forming dinitrosyliron complexes
Sahni, S., Hickok, J. R., & Thomas, D. D. (2018) · Nitric Oxide · doi:10.1016/j.niox.2018.03.003 · Cited by 44 · see citing works
Self-citationHow are nitrosothiols formed de novo in vivo ?
Lancaster, J. R. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.10.015 · Cited by 44 · see citing works
Tsou, C., Tsai, F., Chen, H.-Y., Hsu, I., & Liaw, W. (2013) · Inorganic Chemistry · doi:10.1021/ic302537d · Cited by 43 · see citing works
Is <i>S</i> -Nitrosocysteine a True Surrogate for Nitric Oxide?
Hickok, J. R., Vasudevan, D., Thatcher, G. R. J., & Thomas, D. D. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4543 · Cited by 42 · see citing works
Self-citationFujii, J., & Osaki, T. (2023) · Molecules · doi:10.3390/molecules28020814 · Cited by 42 · see citing works
Dinitrosyl iron complexes with glutathione suppress experimental endometriosis in rats
Burgova, E. N., Tkachev, N. А., Adamyan, L. V., Mikoyan, V. D., Paklina, O. V., Stepanyan, A. A., & Vanin, A. F. (2014) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2014.01.002 · Cited by 39 · see citing works
Keszler, Á., Diers, A. R., Ding, Z., & Hogg, N. (2017) · Nitric Oxide · doi:10.1016/j.niox.2017.01.007 · Cited by 38 · see citing works
Insights into the Diverse Effects of Nitric Oxide on Tumor Biology
Vasudevan, D., & Thomas, D. D. (2014) · Vitamins and hormones · doi:10.1016/b978-0-12-800254-4.00011-8 · Cited by 37 · see citing works
Self-citationKovačević, Ž., Sahni, S., Lok, H. C., Davies, M. J., Wink, D. A., & Richardson, D. R. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.02.021 · Cited by 37 · see citing works
Self-citationLok, H. C., Sahni, S., Jansson, P. J., Kovacevic, Z., Hawkins, C. L., & Richardson, D. R. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.763714 · Cited by 36 · see citing works
Self-citationLok, H. C., Sahni, S., Richardson, V., Kalinowski, D. S., Kovačević, Ž., Lane, D. J. R., & Richardson, D. R. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.07.002 · Cited by 34 · see citing works
Self-citationLiu, T., Zhang, M., Terry, M. H., Schroeder, H. J., Wilson, S. M., Power, G. G., Li, Q., Tipple, T. E., Borchardt, D. B., & Blood, A. B. (2018) · Molecular Pharmacology · doi:10.1124/mol.117.110957 · Cited by 32 · see citing works
Synthetic methodology for preparation of dinitrosyl iron complexes
Cho, S.-L., Liao, C.-J., & Lu, T. (2019) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-019-01668-z · Cited by 32 · see citing works
Nitric oxide and hydrogen sulfide: Sibling rivalry in the family of epigenetic regulators
Kuschman, H. P., Palczewski, M. B., & Thomas, D. D. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.01.010 · Cited by 32 · see citing works
Self-citationLiu, T., Schroeder, H. J., Power, G. G., & Blood, A. B. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102327 · Cited by 30 · see citing works
Toward the Optimization of Dinitrosyl Iron Complexes as Therapeutics for Smooth Muscle Cells
Pectol, D. C., Khan, S. A., Chupik, R. B., Elsabahy, M., Wooley, K. L., Darensbourg, M. Y., & Lim, S. (2019) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.9b00389 · Cited by 30 · see citing works
Vanin, A. F., Pekshev, A. V., Vagapov, A. B., Sharapov, N. A., Lakomkin, V. L., Abramov, A. A., Timoshin, A. A., & Kapelko, V. I. (2021) · BIOPHYSICS · doi:10.1134/s0006350921010218 · Cited by 29 · see citing works
Шумаев, К. Б., Gorudko, I. V., Kosmachevskaya, O. V., Grigorieva, D. V., Panasenko, O. M., Vanin, A. F., Topunov, A. F., Terekhova, M. S., Av, S., Cherenkevich, S. N., et al. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/2798154 · Cited by 29 · see citing works
Thiyl radicals are co-products of dinitrosyl iron complex (DNIC) formation
Truzzi, D. R., Augusto, O., & Ford, P. C. (2019) · Chemical Communications · doi:10.1039/c9cc04454j · Cited by 28 · see citing works
Dynamics of Dinitrosyl Iron Complex (DNIC) Formation with Low Molecular Weight Thiols
Truzzi, D. R., Augusto, O., Iretskii, A. V., & Ford, P. C. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b02338 · Cited by 27 · see citing works
Vanin, A. F. (2020) · Applied Magnetic Resonance · doi:10.1007/s00723-020-01270-6 · Cited by 26 · see citing works
Vanin, A. F. (2017) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-017-0811-8 · Cited by 25 · see citing works
Gusarov, I., & Nudler, E. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.01.022 · Cited by 25 · see citing works
Vanin, A. F., Borodulin, R. R., & Mikoyan, V. D. (2017) · Nitric Oxide · doi:10.1016/j.niox.2017.02.005 · Cited by 25 · see citing works
Pulukkody, R., Kyran, S. J., Bethel, R. D., Hsieh, C., Hall, M. B., Darensbourg, D. J., & Darensbourg, M. Y. (2013) · Journal of the American Chemical Society · doi:10.1021/ja403916v · Cited by 24 · see citing works
Nitrite potentiates the vasodilatory signaling of S-nitrosothiols
Liu, T., Zhang, M., Terry, M. H., Schroeder, H. J., Wilson, S. M., Power, G. G., Li, Q., Tipple, T. E., Borchardt, D., & Blood, A. B. (2018) · Nitric Oxide · doi:10.1016/j.niox.2018.01.011 · Cited by 23 · see citing works
The Fe2(NO)2 Diamond Core: A Unique Structural Motif In Non‐Heme Iron–NO Chemistry
Dong, H. T., Speelman, A. L., Kozemchak, C. E., Sil, D., Krebs, C., & Lehnert, N. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201911968 · Cited by 23 · see citing works
Detection of dinitrosyl iron complexes by ozone-based chemiluminescence
Mukosera, G. T., Liu, T., Ahmed, A. S. I., Li, Q., Sheng, M. H. ‐., Tipple, T. E., Baylink, D. J., Power, G. G., & Blood, A. B. (2018) · Nitric Oxide · doi:10.1016/j.niox.2018.07.005 · Cited by 22 · see citing works
The binuclear form of dinitrosyl iron complexes with thiol-containing ligands in animal tissues
Mikoyan, V. D., Burgova, E. N., Borodulin, R. R., & Vanin, A. F. (2016) · Nitric Oxide · doi:10.1016/j.niox.2016.10.007 · Cited by 22 · see citing works
Burgova, E. N., Tkachev, N. А., Paklina, O. V., Mikoyan, V. D., Adamyan, L. V., & Vanin, A. F. (2014) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2014.07.017 · Cited by 21 · see citing works
Differential mitochondrial dinitrosyliron complex formation by nitrite and nitric oxide
Thomas, D. D., Corey, C. G., Hickok, J. R., Wang, Y., & Shiva, S. (2017) · Redox Biology · doi:10.1016/j.redox.2017.12.007 · Cited by 21 · see citing works
Self-citationMechanisms of Nitric Oxide Reactions Mediated by Biologically Relevant Metal Centers
Ford, P. C., Pereira, J. C. M., & Miranda, K. M. (2013) · Structure and bonding · doi:10.1007/430_2013_117 · Cited by 20 · see citing works
Nitrite and nitroso compounds can serve as specific catalase inhibitors
Titov, V. Y., & Osipov, A. N. (2016) · Redox Report · doi:10.1080/13510002.2016.1168589 · Cited by 18 · see citing works
Mir, J. M., Malik, B. A., & MAURYA, R. C. (2019) · Reviews in Inorganic Chemistry · doi:10.1515/revic-2018-0017 · Cited by 19 · see citing works
Coordination Chemistry of Nitrosyls and Its Biochemical Implications
Lewandowska, H. (2013) · Structure and bonding · doi:10.1007/430_2013_102 · Cited by 19 · see citing works
Vanin, A. F. (2015) · Austin Journal of Reproductive Medicine & Infertility · doi:10.26420/austinjreprodmedinfertil.2015.1019 · Cited by 17 · see citing works
Nitric oxide metabolism in the human placenta during aberrant maternal inflammation
Mukosera, G. T., Clark, T. C., Ngo, L., Liu, T., Schroeder, H. J., Power, G. G., Yellon, S. M., Parast, M. M., & Blood, A. B. (2020) · The Journal of Physiology · doi:10.1113/jp279057 · Cited by 18 · see citing works
Cui, C., Wu, C., Shu, P., Liu, T., Hong Li, A., & Beuve, A. V. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102425 · Cited by 17 · see citing works
Palczewski, M. B., Kuschman, H. P., Hoffman, B. M., Kathiresan, V., Yang, H., Glynn, S. A., Wilson, D. L., Kool, E. T., Montfort, W. R., Chang, J. C., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56928-1 · Cited by 17 · see citing works
Self-citationNitric oxide inhibits FTO demethylase activity to regulate N6-methyladenosine mRNA methylation
Kuschman, H. P., Palczewski, M. B., Hoffman, B. M., Menhart, M., Wang, X., Glynn, S. A., Islam, A. B. M. M. K., Benevolenskaya, E. V., & Thomas, D. D. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102928 · Cited by 16 · see citing works
Self-citationMono- and binuclear dinitrosyl iron complexes with thiol-containing ligands in various biosystems
Vanin, A. F., Mikoyan, V. D., Kubrina, L. N., Borodulin, R. R., & Burgova, E. N. (2015) · BIOPHYSICS · doi:10.1134/s0006350915040247 · Cited by 16 · see citing works
Structural and Electronic Responses to the Three Redox Levels of Fe(NO)N2S2‐Fe(NO)2
Ghosh, P., Ding, S., Quiroz, M., Bhuvanesh, N. S. P., Hsieh, C., Palacios, P. M., Pierce, B. S., Darensbourg, M. Y., & Hall, M. B. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201804168 · Cited by 16 · see citing works
Monomeric Dinitrosyl Iron Complexes: Synthesis and Reactivity
Tran, C. T., Skodje, K. M., & Kim, E. (2014) · Progress in inorganic chemistry · doi:10.1002/9781118869994.ch05 · Cited by 15 · see citing works
Palczewski, M. B., Kuschman, H. P., Bovee, R. C., Hickok, J. R., & Thomas, D. D. (2021) · Biological Chemistry · doi:10.1515/hsz-2020-0323 · Cited by 14 · see citing works
Self-citationMiranda, K. M., Ridnour, L. A., Cheng, R. Y. S., Wink, D. A., & Thomas, D. D. (2023) · Critical Reviews™ in Oncogenesis · doi:10.1615/critrevoncog.2023047302 · Cited by 13 · see citing works
Self-citationThe role of nitric oxide (NO) in the body growth rate of birds
Titov, V. Y., Михайловна, Д. А., Fisinin, V. I., Borkhunova, E. N., Kondratov, G. V., Slesarenko, N. A., & Kochish, I. I. (2018) · World s Poultry Science Journal · doi:10.1017/s0043933918000661 · Cited by 14 · see citing works
Borodulin, R. R., Dereven’kov, I. А., Burbaev, D. S., Makarov, S. V., Mikoyan, V. D., Сереженков, В. А., Kubrina, L. N., Ivanović‐Burmazović, I., & Vanin, A. F. (2014) · Nitric Oxide · doi:10.1016/j.niox.2014.06.005 · Cited by 14 · see citing works
Pulukkody, R., Kyran, S. J., Drummond, M. J., Hsieh, C., Darensbourg, D. J., & Darensbourg, M. Y. (2014) · Chemical Science · doi:10.1039/c4sc01523a · Cited by 13 · see citing works
Ascorbate attenuates red light mediated vasodilation: Potential role of S-nitrosothiols
Keszler, Á., Lindemer, B. J., Hogg, N., & Lohr, N. L. (2018) · Redox Biology · doi:10.1016/j.redox.2018.09.008 · Cited by 13 · see citing works
The Fe2(NO)2 Diamond Core: A Unique Structural Motif In Non‐Heme Iron–NO Chemistry
Dong, H. T., Speelman, A. L., Kozemchak, C. E., Sil, D., Krebs, C., & Lehnert, N. (2019) · Angewandte Chemie · doi:10.1002/ange.201911968 · Cited by 13 · see citing works
Titov, V. Y., Kosenko, O. V., Starkova, E. S., Kondratov, G. V., Borkhunova, E. N., Petrov, V. A., & Osipov, A. N. (2016) · Bulletin of Experimental Biology and Medicine · doi:10.1007/s10517-016-3557-1 · Cited by 12 · see citing works
A Conspectus of Cellular Mechanisms of Nitrosothiol Formation from Nitric Oxide
Li, Q., & Lancaster, J. R. (2012) · Forum on Immunopathological Diseases and Therapeutics · doi:10.1615/forumimmundisther.2012006372 · Cited by 11 · see citing works
Truzzi, D. R., Alves, S. V., Netto, L. E. S., & Augusto, O. (2020) · Antioxidants · doi:10.3390/antiox9040276 · Cited by 11 · see citing works
Development of (NO)Fe(N2S2) as a Metallodithiolate Spin Probe Ligand: A Case Study Approach
Quiroz, M., & Darensbourg, M. Y. (2024) · Accounts of Chemical Research · doi:10.1021/acs.accounts.3c00667 · Cited by 10 · see citing works
Kochish, I. I., Titov, V. Y., Nikonov, I. N., Brazhnik, E. A., Vorobyov, N. I., Korenyuga, M. V., Myasnikova, O. V., Михайловна, Д. А., Griffin, D. K., & Romanov, M. N. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2022.1092242 · Cited by 10 · see citing works
Nitric oxide and thiols: Chemical biology, signalling paradigms and vascular therapeutic potential
Dent, M. R., & DeMartino, A. W. (2023) · British Journal of Pharmacology · doi:10.1111/bph.16274 · Cited by 10 · see citing works
Nitric oxide is an epigenetic regulator of histone post-translational modifications in cancer
Palczewski, M. B., Kuschman, H. P., & Thomas, D. D. (2019) · Current Opinion in Physiology · doi:10.1016/j.cophys.2019.05.006 · Cited by 10 · see citing works
Self-citationEffects of Glutathione and Histidine on NO Release from a Dimeric Dinitrosyl Iron Complex (DNIC)
Pectol, D. C., Khan, S. A., Elsabahy, M., Wooley, K. L., Lim, S., & Darensbourg, M. Y. (2020) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.0c02196 · Cited by 10 · see citing works
- 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 › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review