Quantification of intermediates formed during the reduction of nitrite by deoxyhemoglobin
Open accessAbstract
Nitric oxide (NO) plays a crucial role in human physiology by regulating vascular tone and blood flow. The short life-span of NO in blood requires a mechanism to retain NO bioactivity in the circulation. Recent studies have suggested a mechanism involving the reduction of nitrite back to NO by deoxyhemoglobin in RBCs. A role for RBCs in transporting NO must, however, bypass the scavenging of NO in RBCs by hemoglobin. To understand how the nitrite reaction can deliver bioactive NO to the vasculature, we have studied the intermediates formed during the reaction. A reliable measure of the total concentration of heme-associated nitrite/NO intermediates formed was provided by combining filtration to measure free nitrite by chemiluminescence and electron paramagnetic resonance to measure the final product Hb(II)NO. By modifying the chemiluminescence method used to detect NO, we have been able to identify two intermediates: 1) a heme-associated nitrite complex that is released as NO in acid solution in the presence of ascorbate and 2) an intermediate that releases NO at neutral pH in the presence of ferricyanide when reacted with an Fe(III) ligand like azide. This species designated as "Hb(II)NO(+) (<--)(-->)Hb(III)NO" has properties of both isomeric forms resulting in a slower NO dissociation rate and much higher stability than Hb(III)NO, but provides a potential source for bioactive NO, which can be released from the RBC. This detailed analysis of the nitrite reaction with deoxyHb provides important insights into the mechanism for nitrite induced vasodilation by RBCs.
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Several proposed mechanisms explain how nitrite-derived bioactivity can be exported from the red blood cell, generally involving either a compartment model with submembrane localization or formation of another nitrogen oxide such as a nitrosothiol or N2O3.
“Several proposed mechanisms have been constructed to explain how nitrite-derived bioactivity can be exported from the red blood cell and these generally involve either a compartment model with submembrane localization of the reaction allowing for inefficient free NO escape, or the formation of another nitrogen oxide such as a nitrosothiol or N2O3 that can get out of the red blood cell and carry NO”
From Mechanisms of nitrite bioactivation (2014) · cites this paper as [49]
In one proposed mechanism for nitrite anhydrase, an intermediate ferric nitrosyl species is formed and this then reacts with a second nitrite molecule.
“In one proposed mechanism for nitrite anhydrase, an intermediate ferric nitrosyl species is formed (which is equivalent to a ferrous nitrosonium) and this then reacts with a second nitrite molecule [49, 97, 98].”
From Mechanisms of nitrite bioactivation (2014) · cites this paper as [49]
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Nitrite reduction to nitric oxide by deoxyhemoglobin vasodilates the human circulation
Cosby, K., Partovi, K. S., Crawford, J. H., Patel, R. P., Reiter, C. D., Martyr, S., Yang, B. K., Waclawiw, M. A., Zalos, G., Xu, X., et al. (2003) · Nature Medicine · doi:10.1038/nm954 · Cited by 1,807 · see citing works
S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
Jia, L., Bonaventura, C., Bonaventura, J., & Stamler, J. S. (1996) · Nature · doi:10.1038/380221a0 · Cited by 1,586 · see citing works
Nitric Oxide as a Signaling Molecule in the Vascular System: An Overview
Ignarro, L. J., Cirino, G., Casini, A., & Claudio Napoli, A. (1999) · Journal of Cardiovascular Pharmacology · doi:10.1097/00005344-199912000-00016 · Cited by 765 · see citing works
Export by red blood cells of nitric oxide bioactivity
Pawloski, J. R., Hess, D. T., & Stamler, J. S. (2001) · Nature · doi:10.1038/35054560 · Cited by 579 · see citing works
Diffusion-limited reaction of free nitric oxide with erythrocytes
Liu, X., Miller, M. J. S., Joshi, M. S., Sadowska-Krowicka, H., Clark, D. A., & Lancaster, J. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.30.18709 · Cited by 512 · see citing works
Nitric oxide in the human respiratory cycle
McMahon, T., Moon, R. E., Luschinger, B. P., Carraway, M. S., Stone, A. E., Stolp, B. W., Gow, A. J., Pawloski, J. R., Watke, P., Singel, D. J., et al. (2002) · Nature Medicine · doi:10.1038/nm718 · Cited by 462 · see citing works
Erythrocytes are the major intravascular storage sites of nitrite in human blood
Dejam, A. (2005) · Blood · doi:10.1182/blood-2005-02-0567 · Cited by 350 · see citing works
Nagababu, E., Ramasamy, S., Abernethy, D. R., & Rifkind, J. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307572200 · Cited by 349 · see citing works
Self-citationNO Generation From Nitrite and Its Role in Vascular Control
Lundberg, J. O., & Weitzberg, E. (2005) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000161048.72004.c2 · Cited by 341 · see citing works
Kinetics and mechanism of the oxidation of human deoxyhemoglobin by nitrites.
Doyle, M. P., Pickering, R. A., DeWeert, T. M., Hoekstra, J. W., & Pater, D. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43285-1 · Cited by 334 · see citing works
Gladwin, M. T., Ognibene, F. P., Pannell, L. K., Nichols, J. S., Pease‐Fye, M. E., Shelhamer, J. H., & Schechter, A. N. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.180155397 · Cited by 274 · see citing works
The Reaction between Nitrite and Deoxyhemoglobin
Huang, K. T., Keszler, A., Patel, N., Patel, R. P., Gladwin, M. T., Kim-Shapiro, D. B., & Hogg, N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501496200 · Cited by 253 · see citing works
Reaction of nitric oxide with heme proteins and model compounds of hemoglobin
Sharma, V. S., Traylor, T. G., Gardiner, R., & Mizukami, H. (1987) · Biochemistry · doi:10.1021/bi00387a015 · Cited by 245 · see citing works
An <i>S</i> -nitrosothiol (SNO) synthase function of hemoglobin that utilizes nitrite as a substrate
Angelo, M., Singel, D. J., & Stamler, J. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600942103 · Cited by 233 · see citing works
Hoshino, M., Maeda, M., Konishi, R., Seki, H., & Ford, P. C. (1996) · Journal of the American Chemical Society · doi:10.1021/ja953311w · Cited by 219 · see citing works
Luchsinger, B. P., Rich, E. N., Gow, A. J., Williams, E. M., Stamler, J. S., & Singel, D. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0233287100 · Cited by 202 · see citing works
Kim‐Shapiro, D. B., Gladwin, M. T., Patel, R. P., & Hogg, N. (2004) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2004.10.034 · Cited by 172 · see citing works
Gladwin, M. T., Wang, X., Reiter, C. D., Yang, B. K., Vivas, E. X., Bonaventura, C., & Schechter, A. N. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203236200 · Cited by 160 · see citing works
Endothelial nitric oxide synthase reduces nitrite anions to NO under anoxia
Gautier, C., van Faassen, E., Mikula, I., Martasek, P., & Slama-Schwok, A. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.01.031 · Cited by 143 · see citing works
Nitrosyliron(III) hemoglobin: autoreduction and spectroscopy
Addison, A. W., & Stephanos, J. J. (1986) · Biochemistry · doi:10.1021/bi00362a018 · Cited by 96 · see citing works
Luchsinger, B. P., Rich, E. N., Yan, Y., Williams, E. M., Stamler, J. S., & Singel, D. J. (2005) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2004.12.010 · Cited by 89 · see citing works
Nagababu, E., Ramasamy, S., & Rifkind, J. M. (2006) · Nitric Oxide · doi:10.1016/j.niox.2006.01.012 · Cited by 86 · see citing works
Self-citationNagababu, E., & Rifkind, J. M. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.12.029 · Cited by 79 · see citing works
Self-citationWang, Y., & Averill, B. A. (1996) · Journal of the American Chemical Society · doi:10.1021/ja9538647 · Cited by 54 · see citing works
Autocatalytic Oxidation of Hemoglobin by Nitrite: A Possible Mechanism
Lissi, E. A. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00004-5 · Cited by 45 · see citing works
Nagababu, E., Ramasamy, S., & Rifkind, J. M. (2007) · Biochemistry · doi:10.1021/bi700364e · Cited by 33 · see citing works
Self-citationNitric Oxide Redox Reactions and Red Cell Biology
Rifkind, J. M., Nagababu, E., & Ramasamy, S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1193 · Cited by 28 · see citing works
Self-citationSerial measurements of whole blood nitrite in an intensive care setting
Kehmeier, E. S., Kropp, M., Kleinbongard, P., Lauer, T., Balzer, J., Merx, M. W., Heusch, G., Kelm, M., Lepper, W., & Rassaf, T. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.02.014 · Cited by 16 · see citing works
The ferric form of the three human embryonic hemoglobins and their reactions with azide ions
Brittain, T. (2000) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(00)00116-1 · Cited by 8 · see citing works
Flagged first, then by citations
Research works printed but not linked: 5
- Luchsinger, B. P., Rich, E. N., Gow, A. J., Williams, E. M., Stamler, J. S., and Singel, D. J. (2003) Proc. Natl. Acad. Sci. U. S. A. 100, 461-466
- Gladwin, M. T., Ognibene, F. P., Pannell, L. K., Nichols, J. S., Pease-Fye, M. E., Shelhamer, J. H., and Schechter, A. N. (2000) Proc. Natl. Acad. Sci.
- Addison, A. W., and Stephanos, J. J. (1986) Biochemistry 25, 4104 -4113
- Angelo, M., Singel, D. J., and Stamler, J. S. (2006) Proc. Natl. Acad. Sci.
- Nagababu, E., Cao, Z., Ramasamy, S., and Rifkind, J. M. (2008) XVth Inter- national Conference on Oxygen Binding and Sensing Proteins P27
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Maia, L. B., & Moura, J. J. G. (2014) · Chemical Reviews · doi:10.1021/cr400518y · Cited by 401 · see citing works
Fukuto, J. M., Carrington, S. J., Tantillo, D. J., Harrison, J. G., Ignarro, L. J., Freeman, B. A., Chen, A., & Wink, D. A. (2012) · Chemical Research in Toxicology · doi:10.1021/tx2005234 · Cited by 389 · see citing works
Kapil, V., Khambata, R. S., Jones, D. A., Rathod, K., Primus, C., Massimo, G., Fukuto, J. M., & Ahluwalia, A. (2020) · Pharmacological Reviews · doi:10.1124/pr.120.019240 · Cited by 248 · see citing works
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Cao, Z., Bell, J. B., Mohanty, J. G., Nagababu, E., & Rifkind, J. M. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01233.2008 · Cited by 90 · see citing works
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Liu, C., Wajih, N., Liu, X., Basu, S., Janes, J., Marvel, M., Keggi, C., Helms, C. C., Lee, A. N., Belanger, A. M., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.609222 · Cited by 76 · see citing works
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Waltz, P., Escobar, D., Botero, A. M., & Zuckerbraun, B. S. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2015.6256 · Cited by 70 · see citing works
Vitturi, D. A., & Patel, R. P. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.05.037 · Cited by 59 · see citing works
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- Authors
- Salgado, M. T., Nagababu, E., & Rifkind, J. M.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Rifkind, Joseph M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-05
- Volume
- 284
- Issue
- 19
- Pages
- 12710-12718
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2676000
- OpenAlex
- W2056208513
- Cited by
- 56
- References
- 29
- Citations by year
- 2023: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 3 · 2017: 2 · 2016: 1 · 2015: 4 · 2014: 6 · 2013: 4 · 2012: 17
- FWCI
- 4.75
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Keywords
- nitrite reduction, deoxyhemoglobin, nitric oxide, erythrocytes, electron spin resonance, vitamin C, ferricyanide, azide
- MeSH terms
- Electron Spin Resonance Spectroscopy, Erythrocytes, Hemoglobins, Humans, Isomerism, Nitrates, Nitrites, Oxidation-Reduction, Luminescence
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