Red Blood Cell Membrane-Facilitated Release of Nitrite-Derived Nitric Oxide Bioactivity
Abstract
The reduction of nitrite by deoxyhemoglobin to nitric oxide (NO) has been proposed as a mechanism for the transfer of NO bioactivity from the red blood cell (RBC) to the vasculature. This transfer can increase vascular dilatation. The major challenge to this hypothesis is the very efficient scavenging of NO by hemoglobin, which prevents the release of NO from RBCs. Previous studies indicate that the reaction of nitrite with deoxyhemoglobin produces two metastable intermediates involving nitrite bound to deoxyhemoglobin and a hybrid intermediate [Hb(II)NO(+) ↔ Hb(III)NO] where the nitrite is reduced, but unavailable to react with hemoglobin. We have now shown how unique properties of these intermediates provide a pathway for the release of NO bioactivity from RBCs. The high membrane affinity of these intermediates (>100-fold greater than that of deoxyhemoglobin) places these intermediates on the membrane. Furthermore, membrane-induced conformational changes of the nitrite-reacted intermediates facilitate the release of NO from the hybrid intermediate and nitrite from the nitrite-bound intermediate. Increased membrane affinity, coupled with facilitated dissociation of NO and nitrite from the membrane-bound intermediates, provides the first realistic mechanism for the potential release of NO and nitrite from the RBC and their potential transfer to the vasculature.
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Red blood cells play a pivotal role in facilitating nitrite reduction via deoxyhaemoglobin, especially in hypoxic and acidic conditions, enabling targeted delivery of NO to oxygen-deprived tissues.
“Red blood cells (RBCs) play a pivotal role in facilitating nitrite reduction via deoxyhaemoglobin, especially in hypoxic and acidic conditions. This enables the targeted delivery of NO to oxygen-deprived tissues [82].”
From Dietary Nitrate-Rich Vegetables as Natural Modulators of Health: Mechanisms and Benefits in Ageing Populations (2026) · cites this paper as [82]
Beetroot is one of the richest dietary sources of inorganic nitrate (250-400 mg/100 g fresh weight), depending on agronomic and storage conditions.
“Depending on agronomic and storage conditions, it is also one of the richest dietary sources of inorganic nitrate (250–400 mg/100 g fresh weight) [80,81,82,83,84,85,86,87,88,89,90,91,92,93,94,95].”
From Dietary Nitrate-Rich Vegetables as Natural Modulators of Health: Mechanisms and Benefits in Ageing Populations (2026) · cites this paper as [82]
Cites
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
Blood Flow Regulation by <i>S</i> -Nitrosohemoglobin in the Physiological Oxygen Gradient
Stamler, J. S., Jia, L., Eu, J. P., McMahon, T. J., Demchenko, I. T., Bonaventura, J., Gernert, K., & Piantadosi, C. A. (1997) · Science · doi:10.1126/science.276.5321.2034 · Cited by 1,050 · 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
Mechanism of NO-induced oxidation of myoglobin and hemoglobin
Eich, R. F., Li, T., Lemon, D. D., Doherty, D. H., Curry, S. R., Aitken, J. F., Mathews, A. J., Johnson, K. A., Smith, R. D., Phillips, et al. (1996) · Biochemistry · doi:10.1021/bi960442g · Cited by 613 · see citing works
Red blood cells express a functional endothelial nitric oxide synthase
Kleinbongard, P. (2005) · Blood · doi:10.1182/blood-2005-10-3992 · Cited by 566 · 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
Reduction of nitrite to nitric oxide catalyzed by xanthine oxidoreductase
Godber, B. L. J., Doel, J. J., Sapkota, G. P., Blake, D. R., Stevens, C. R., Eisenthal, R., & Harrison, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.7757 · Cited by 411 · see citing works
The biochemistry of nitric oxide, nitrite, and hemoglobin: role in blood flow regulation
Gladwin, M. T., Crawford, J. H., & Patel, R. P. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.11.032 · Cited by 378 · 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-citationNitrite reductase activity is a novel function of mammalian mitochondria
Kozlov, A. V., Staniek, K., & Nohl, H. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00788-7 · Cited by 342 · 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., Raat, N. J. H., Shiva, S., Dezfulian, C., Hogg, N., Kim-Shapiro, D. B., & Patel, R. P. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00407.2006 · Cited by 329 · see citing works
Red blood cell regulation of microvascular tone through adenosine triphosphate
Dietrich, H. H., Ellsworth, M. L., Sprague, R. S., & Dacey, R. G. (2000) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2000.278.4.h1294 · Cited by 278 · see citing works
Nitric Oxide Production from Nitrite Occurs Primarily in Tissues Not in the Blood
Li, H., Cui, H., Kundu, T. K., Alzawahra, W., & Zweier, J. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801785200 · Cited by 269 · 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
Catalytic generation of N2O3 by the concerted nitrite reductase and anhydrase activity of hemoglobin
Basu, S., Grubina, R., Huang, J., Conradie, J., Huang, Z., Jeffers, A., Jiang, A., He, X., Azarov, I., Seibert, R., et al. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.46 · Cited by 224 · see citing works
Tissue Processing of Nitrite in Hypoxia
Feelisch, M., Fernandez, B. O., Bryan, N. S., Garcia-Saura, M. F., Bauer, S., Whitlock, D. R., Ford, P. C., Janero, D. R., Rodriguez, J., & Ashrafian, H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806654200 · Cited by 218 · see citing works
Determination of Km for oxygen of nitric oxide synthase isoforms.
Rengasamy, A., & Johns, R. A. (1996) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)12266-0 · Cited by 148 · see citing works
Grubina, R., Huang, Z., Shiva, S., Joshi, M. S., Azarov, I., Basu, S., Ringwood, L. A., Jiang, A., Hogg, N., Kim‐Shapiro, D. B., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700546200 · Cited by 147 · 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
Production of Superoxide from Hemoglobin-Bound Oxygen Under Hypoxic Conditions
Balagopalakrishna, C., Manoharan, P. T., Abugo, O. O., & Rifkind, J. M. (1996) · Biochemistry · doi:10.1021/bi952875+ · Cited by 130 · see citing works
Self-citationBramley, T. A., COLEMAN, R., & FINEAN, J. B. (1971) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(71)90003-4 · Cited by 104 · see citing works
Observation of the Dissociation of Unliganded Hemoglobin
Thomas, J. O., & Edelstein, S. J. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)81781-5 · Cited by 91 · see citing works
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
Self-citationDiminished NO release in chronic hypoxic human endothelial cells
Østergaard, L., Stankevıčıus, E., Andersen, M. R., Eskildsen-Helmond, Y. E. G., Ledet, T., Mulvany, M. J., & Simonsen, U. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01230.2006 · Cited by 80 · see citing works
Nagababu, 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-citationMechanical stimulation of nitric oxide synthesizing mechanisms in erythrocytes
Ülker, P., Satı, L., Çelik-Özenci, Ç., Meiselman, H. J., & Baskurt, O. K. (2009) · Biorheology · doi:10.3233/bir-2009-0532 · Cited by 78 · see citing works
Nitric oxide from nitrite reduction by hemoglobin in the plasma and erythrocytes
Chen, K., Piknova, B., Pittman, R. N., Schechter, A. N., & Popel, A. S. (2007) · Nitric Oxide · doi:10.1016/j.niox.2007.09.088 · Cited by 63 · see citing works
Balagopalakrishna, C., Abugo, O. O., Horsky, J., Manoharan, P. T., Nagababu, E., & Rifkind, J. M. (1998) · Biochemistry · doi:10.1021/bi980941c · Cited by 60 · see citing works
Self-citationQuantification of intermediates formed during the reduction of nitrite by deoxyhemoglobin
Salgado, M. T., Nagababu, E., & Rifkind, J. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808647200 · Cited by 56 · see citing works
Self-citationHalpin, S. T., & Spence, D. M. (2010) · Analytical Chemistry · doi:10.1021/ac101130s · Cited by 38 · see citing works
A new mode for heme-heme interactions in hemoglobin associated with distal perturbations
Levy, A., Sharma, V., Zhang, L., & Rifkind, J. M. (1992) · Biophysical Journal · doi:10.1016/s0006-3495(92)81879-9 · Cited by 35 · see citing works
Self-citationDemehin, A. A., Abugo, O. O., Rajadas, J., Lakowicz, J. R., & Rifkind, J. M. (2002) · Biochemistry · doi:10.1021/bi012007e · Cited by 34 · see citing works
Self-citationNirmala, R., & Rifkind, J. M. (1999) · Biophysical Journal · doi:10.1016/s0006-3495(99)77340-6 · Cited by 33 · see citing works
Self-citationWiltrout, M. E., Giovannelli, J. L., Simplăceanu, V., Lukin, J. A., Ho, N. T., & Ho, C. (2005) · Biochemistry · doi:10.1021/bi048289a · Cited by 28 · see citing works
Rifkind, J. M., Nagababu, E., Dobrosielski, D. A., Salgado, M. T., Lima, M., Ouyang, P., & Silber, H. A. (2014) · Nitric Oxide · doi:10.1016/j.niox.2014.06.007 · Cited by 21 · see citing works
Self-citationA New Paramagnetic Intermediate Formed during the Reaction of Nitrite with Deoxyhemoglobin
Salgado, M. T., Ramasamy, S., Tsuneshige, A., Manoharan, P. T., & Rifkind, J. M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja1115088 · Cited by 20 · see citing works
Self-citationRifkind, J. M., Nagababu, E., & Ramasamy, S. (2011) · Nitric Oxide · doi:10.1016/j.niox.2011.01.001 · Cited by 14 · see citing works
Self-citationRegulation of Oxygen Delivery by the Reaction of Nitrite with RBCs Under Hypoxic Conditions
Rifkind, J. M., Salgado, M. T., & Cao, Z. (2011) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-1566-4_27 · Cited by 6 · see citing works
Self-citation
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Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works
Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia
Kuhn, V., Diederich, L., Keller, T. C. S., Kramer, C. M., Lückstädt, W., Panknin, C., Suvorava, T., Isakson, B. E., Kelm, M., & Cortese-Krott, M. M. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6954 · Cited by 469 · see citing works
Erythrocytes and Vascular Function: Oxygen and Nitric Oxide
Helms, C. C., Gladwin, M. T., & Kim‐Shapiro, D. B. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00125 · Cited by 166 · see citing works
Red blood cell dysfunction: a new player in cardiovascular disease
Pernow, J., Mahdi, A., Yang, J., & Zhou, Z. (2019) · Cardiovascular Research · doi:10.1093/cvr/cvz156 · Cited by 163 · see citing works
Hazegh, K. E., Fang, F., Bravo, M. D., Tran, J. Q., Muench, M. O., Jackman, R. P., Roubinian, N. H., Bertolone, L., D’Alessandro, A., Dumont, L. J., et al. (2020) · Transfusion · doi:10.1111/trf.16168 · Cited by 61 · see citing works
Erkens, R., Suvorava, T., Kramer, C. M., Diederich, L., Kelm, M., & Cortese-Krott, M. M. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6904 · Cited by 53 · see citing works
Hirsch, R. E., Sibmooh, N., Fucharoen, S., & Friedman, J. M. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6806 · Cited by 48 · see citing works
Nitric oxide in red blood cell adaptation to hypoxia
Zhao, Y., Wang, X., Noviana, M., & Hou, M. (2018) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmy055 · Cited by 46 · see citing works
How 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
The NO-heme signaling hypothesis
Kleschyov, A. L. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.08.025 · Cited by 40 · see citing works
The role of globins in cardiovascular physiology
Keller, T. C. S., Lechauve, C., Keller, A., Brooks, S., Weiss, M. J., Columbus, L. M., Ackerman, H. C., Cortese-Krott, M. M., & Isakson, B. E. (2021) · Physiological Reviews · doi:10.1152/physrev.00037.2020 · Cited by 37 · see citing works
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Dent, M. R., DeMartino, A. W., Tejero, J., & Gladwin, M. T. (2021) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.1c01048 · Cited by 35 · see citing works
Thiol-catalyzed formation of NO-ferroheme regulates intravascular NO signaling
DeMartino, A. W., Poudel, L., Dent, M. R., Chen, X., Xu, Q., Gladwin, B., Tejero, J., Basu, S., Alipour, E., Jiang, Y., et al. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01413-3 · Cited by 35 · see citing works
Rifkind, J. M., Mohanty, J. G., Nagababu, E., Salgado, M. T., & Cao, Z. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00690 · Cited by 27 · see citing works
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Helms, C. C., Liu, X., & Kim‐Shapiro, D. B. (2016) · Biological Chemistry · doi:10.1515/hsz-2016-0263 · Cited by 23 · see citing works
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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 Impact of Surgery and Stored Red Blood Cell Transfusions on Nitric Oxide Homeostasis
Nagababu, E., Scott, A. V., Johnson, D. J., Goyal, A., Lipsitz, J. A., Barodka, V. M., Berkowitz, D. E., & Frank, S. M. (2016) · Anesthesia & Analgesia · doi:10.1213/ane.0000000000001392 · Cited by 12 · see citing works
Self-citationSrihirun, S., Piknova, B., Sibmooh, N., & Schechter, A. N. (2018) · PLoS ONE · doi:10.1371/journal.pone.0193747 · Cited by 13 · see citing works
Diosmin and Bromelain Stimulate Glutathione and Total Thiols Production in Red Blood Cells
Gwoździński, Ł., Bernasinska-Slomczewska, J., Wiktorowska‐Owczarek, A., Kowalczyk, E., & Pieniążek, A. (2023) · Molecules · doi:10.3390/molecules28052291 · Cited by 11 · see citing works
Chen, X., Lin, G., Dai, C., & Xu, K. (2023) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2023.1069864 · Cited by 9 · see citing works
Wang, L., & Cai, Q. (2019) · PubMed Central · doi:10.7499/j.issn.1008-8830.2019.11.005 · Cited by 8 · see citing works
Anemia contributes to cardiovascular disease through reductions in nitric oxide
Andreotti, F., Coluzzi, G., Pafundi, T., Rio, T., Navarese, E. P., Crea, F., Pistolesi, M., Maseri, A., & Hennekens, C. H. (2016) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00995.2015 · Cited by 7 · see citing works
Red Blood Cells: A Newly Described Partner in Central Retinal Vein Occlusion Pathophysiology?
Laurance, S., Marin, M., & Colin, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021072 · Cited by 6 · see citing works
Liu, H., Li, J., Wu, N., She, Y., Luo, Y., Huang, Y., Quan, H., Fu, W., Li, X., Zeng, D., et al. (2024) · Inflammation · doi:10.1007/s10753-023-01932-0 · Cited by 5 · see citing works
Buerk, D. G., Liu, Y., Zaccheo, K. A., Barbee, K. A., & Jaron, D. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.01053 · Cited by 5 · see citing works
Cortese-Krott, M. M., Kramer, C. M., & Kelm, M. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-804273-1.00014-4 · Cited by 5 · see citing works
Role of hydrogen sulfide in catalyzing the formation of NO-ferroheme
Poudel, L., Karunarathna, T. S., Baker, S. R., Alipour, E., Dent, M. R., Tejero, J., Gladwin, M. T., DeMartino, A. W., & Kim‐Shapiro, D. B. (2025) · Nitric Oxide · doi:10.1016/j.niox.2025.09.002 · Cited by 5 · see citing works
Rao, S., Zhang, J., Lin, J., Wan, J., & Chen, Y. (2022) · Journal of Clinical Medicine · doi:10.3390/jcm11247373 · Cited by 4 · see citing works
The role of red blood cell distribution width (RDW) in the diagnosis of pediatric sepsis
Xu, L., Yuan, L., Chi, K., Zhong, D., & Huang, L. (2023) · The Turkish Journal of Pediatrics · doi:10.24953/turkjped.2023.182 · Cited by 3 · see citing works
Kurhaluk, N., Kołodziejska, R., Buyun, L., Kamiński, P., & Tkaczenko, H. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27083461 · Cited by 3 · see citing works
“This enables the targeted delivery of NO to oxygen-deprived tissues [82].”
Li, M.-J., Lu, Z.-H., Cao, L.-J., & Sun, Y. (2026) · PLoS ONE · doi:10.1371/journal.pone.0343684 · Cited by 2 · see citing works
Dudok, K. P., Burda, V. A., Liuta, M. Y., Fedorovych, A. ;. Л. Н. У. І. І. Ф., Bilyi, O. I., Yefimenko, N. V., Kaniuka, O., & Sybirna, N. O. (2017) · Studia Biologica · doi:10.30970/sbi.1102.527 · Cited by 2 · see citing works
Taranikanti, M., Varatharajan, S., John, N. A., Ganji, V., Madhusudhan, U., Medala, K., Archana Gaur, T., & Ansari, A. (2025) · Indian Journal of Cardiovascular Disease in Women · doi:10.25259/ijcdw_105_2024
Flavonoids: Hemorheological effects and mechanisms of action
Анищенко, А. М., Алиев, О. И., & Плотников, М. Б. (2026) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-026-05763-2
- Authors
- Salgado, M. T., Cao, Z., Nagababu, E., Mohanty, J. G., & Rifkind, J. M.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Rifkind, Joseph M.
- ORCID
- Cao, Zeling
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2015-10-28
- Volume
- 54
- Issue
- 44
- Pages
- 6712-6723
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2433011679
- Cited by
- 34
- References
- 41
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 1 · 2023: 5 · 2022: 1 · 2021: 2 · 2020: 1 · 2019: 2 · 2018: 6 · 2017: 4 · 2016: 7
- FWCI
- 3.02
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging
- 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
- nitric oxide release, nitrite, deoxyhemoglobin, erythrocyte membrane, nitrite reduction, membrane affinity, conformational change, vascular system, vascular dilation
- MeSH terms
- Erythrocyte Membrane, Hemoglobins, Humans, Nitric Oxide, Nitrites, Oxidation-Reduction
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