Reactivity of glass-embedded met hemoglobin derivatives toward external NO: implications for nitrite-mediated production of bioactive NO
Open accessAbstract
Many protein reactions are exceedingly difficult to dissect under standard conditions due to low concentrations of reactants and intermediates. A case in point are several proposed reactions of hemoglobin with both nitrite and nitric oxide. In the present work, glassy matrices are used to dynamically control the rate at which externally introduced gaseous NO accesses and reacts with several different met Hb derivatives including the nitrite, nitrate, and aquomet forms. This novel yet general approach reveals a clear difference between nitrite and other ligands including nitrate, water, and an internal imidazole. For nitrate, water, and the internal distal imidazole, the observed spectral changes indicate that NO entering the distal heme pocket is effective in displacing these ligands from the ferric heme iron. In contrast, when the ligand is nitrite, the resulting initial spectra indicate the formation of an intermediate that has distinctly ferrous-like properties. The spectrum and the response of DAF fluorescence to the presence of the intermediate are consistent with a recently proposed nitrite anhydrase reaction. This proposed intermediate is especially significant in that it represents a pathway for a nitrite-dependent catalytic process whereby Hb generates relatively long-lived bioactive forms of NO such as S-nitrosoglutathione. The failure to form this intermediate either at low pH or when the glass is extensively dried is consistent with the requirement for a specific conformation of reactants and residue side chains within the distal heme pocket.
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?
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 [51]
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
Detection and Imaging of Nitric Oxide with Novel Fluorescent Indicators: Diaminofluoresceins
Kojima, H., Nakatsubo, N., Kikuchi, K., Kawahara, S., Kirino, Y., Nagoshi, H., Hirata, Y., & Nagano, T. (1998) · Analytical Chemistry · doi:10.1021/ac9801723 · Cited by 1,391 · see citing works
Ignarro, L. J., Fukuto, J. M., Griscavage, J. M., Rogers, N. E., & Byrns, R. E. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.8103 · Cited by 856 · see citing works
Slaving: Solvent fluctuations dominate protein dynamics and functions
Fenimore, P. W., Frauenfelder, H., McMahon, B. H., & Parak, F. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212637899 · Cited by 677 · see citing works
Reactions between nitric oxide and haemoglobin under physiological conditions
Gow, A. J., & Stamler, J. S. (1998) · Nature · doi:10.1038/34402 · Cited by 562 · see citing works
Fenimore, P. W., Frauenfelder, H., McMahon, B. H., & Young, R. D. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405573101 · Cited by 524 · see citing works
Herold, S., Exner, M., & Nauser, T. (2001) · Biochemistry · doi:10.1021/bi002407m · Cited by 324 · see citing works
Unraveling the Reactions of Nitric Oxide, Nitrite, and Hemoglobin in Physiology and Therapeutics
Kim-Shapiro, D. B., Schechter, A. N., & Gladwin, M. T. (2006) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000204350.44226.9a · Cited by 308 · see citing works
Protein folding is slaved to solvent motions
Frauenfelder, H., Fenimore, P. W., Chen, G., & McMahon, B. H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607168103 · Cited by 286 · 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
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
Protein Reaction Kinetics in a Room-Temperature Glass
Hagen, S. J., Hofrichter, J., & Eaton, W. A. (1995) · Science · doi:10.1126/science.7638618 · Cited by 208 · see citing works
Gladwin, M. T., Grubina, R., & Doyle, M. P. (2009) · Accounts of Chemical Research · doi:10.1021/ar800089j · Cited by 194 · see citing works
Hydration, slaving and protein function
Frauenfelder, H., Fenimore, P. W., & McMahon, B. H. (2002) · Biophysical Chemistry · doi:10.1016/s0301-4622(02)00083-2 · Cited by 129 · see citing works
Internal dynamics and protein–matrix coupling in trehalose-coated proteins
Cordone, L., Cottone, G., Giuffrida, S., Palazzo, G., Venturoli, G., & Viappiani, C. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.03.004 · Cited by 121 · see citing works
Evidence for Damped Hemoglobin Dynamics in a Room Temperature Trehalose Glass
Gottfried, D. S., Peterson, E. S., Sheikh, A. G., et al. (1996) · The Journal of Physical Chemistry · doi:10.1021/jp9609489 · Cited by 114 · 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
A reduction of protein specific motions in co-ligated myoglobin embedded in a trehalose glass
Cordone, L., Galajda, P., Vitrano, E., et al. (1998) · European Biophysics Journal · doi:10.1007/s002490050123 · Cited by 87 · see citing works
Protein dynamics and function: Insights from the energy landscape and solvent slaving
Frauenfelder, H., Fenimore, P. W., & Young, R. D. (2007) · IUBMB Life · doi:10.1080/15216540701194113 · Cited by 72 · see citing works
Librizzi, F., Viappiani, C., Abbruzzetti, S., et al. (2002) · The Journal of Chemical Physics · doi:10.1063/1.1426409 · Cited by 64 · see citing works
Reactions of Nitric Oxide with Amines in the Presence of Dioxygen
Nagano, T., Takizawa, H., & Hirobe, M. (1995) · Tetrahedron Letters · doi:10.1016/0040-4039(95)01715-t · Cited by 63 · see citing works
Dantsker, D., Samuni, U., Friedman, J. M., et al. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.04.002 · Cited by 56 · 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
Reactions of Nitric Oxide with Amines in the Presence of Dioxygen
NAGANO, T. (1995) · Tetrahedron Letters · doi:10.1016/00404-0399(50)1715t- · Cited by 53 · see citing works
Lui, F. E., Dong, P., & Kluger, R. (2008) · Biochemistry · doi:10.1021/bi801116k · Cited by 49 · see citing works
Dantsker, D., Roche, C. J., Samuni, U., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506333200 · 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
Samuni, U., Dantsker, D., Roche, C. J., & Friedman, J. M. (2007) · Gene · doi:10.1016/j.gene.2007.04.032 · Cited by 31 · see citing works
Self-citationSamuni, U., Roche, C. J., Dantsker, D., et al. (2007) · Journal of the American Chemical Society · doi:10.1021/ja072342b · Cited by 30 · see citing works
Trehalose Glass-Facilitated Thermal Reduction of Metmyoglobin and Methemoglobin
Ray, A., Friedman, B. A., & Friedman, J. M. (2002) · Journal of the American Chemical Society · doi:10.1021/ja0201348 · Cited by 27 · see citing works
Self-citationNavati, M. S., & Friedman, J. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606866200 · Cited by 24 · see citing works
Self-citationPegylated hemoglobins mechanisms to avoid vasoconstriction and maintain perfusion
Cabrales, P., & Friedman, J. M. (2007) · Transfusion Alternatives in Transfusion Medicine · doi:10.1111/j.1778-428x.2007.00090.x · Cited by 17 · see citing works
Self-citationHagen, S. J., Hofrichter, H. J., Bunn, H. F., et al. (1995) · Transfusion Clinique et Biologique · doi:10.1016/s1246-7820(05)80066-7 · Cited by 10 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- [1]Kim-Shapiro DB Schechter AN Gladwin MT Arterioscler Thromb Vasc Biol 2006 26 697 705 16424350
Cited by
Sorted by citations
Obstructive sleep apnoea and its cardiovascular consequences
Bradley, T. D., & Floras, J. S. (2009) · The Lancet · doi:10.1016/s0140-6736(08)61622-0 · Cited by 1,385 · see citing works
Maia, L. B., & Moura, J. J. G. (2014) · Chemical Reviews · doi:10.1021/cr400518y · Cited by 401 · see citing works
Mechanisms of nitrite bioactivation
Kim-Shapiro, D. B., & Gladwin, M. T. (2014) · Nitric Oxide · doi:10.1016/j.niox.2013.11.002 · Cited by 157 · see citing works
Reactions of NO and nitrite with heme models and proteins
Ford, P. C. (2010) · Inorganic Chemistry · doi:10.1021/ic902073z · Cited by 138 · see citing works
NO reactions with sol-gel and solution phase samples of the ferric nitrite derivative of HbA
Roche, C. J., & Friedman, J. M. (2010) · Nitric Oxide · doi:10.1016/j.niox.2009.11.003 · Cited by 19 · see citing works
Navati, M. S., & Friedman, J. M. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp909425z · Cited by 12 · see citing works
Self-citation
- Authors
- Navati, M. S., & Friedman, J. M.
- Affiliations
- Albert Einstein College of Medicine (US)
- Corresponding author
- Friedman, Joel M.
- ORCID
- Friedman, Joel M.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2009-08-10
- Volume
- 131
- Issue
- 34
- Pages
- 12273-12279
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- PMC
- PMC2743724
- OpenAlex
- W2013015333
- Cited by
- 28
- References
- 32
- Citations by year
- 2024: 1 · 2018: 2 · 2017: 1 · 2016: 2 · 2015: 3 · 2014: 3 · 2013: 5 · 2012: 2
- FWCI
- 1.48
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of the American Chemical Society (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (5p01hl071064-05)
- National Heart, Lung, and Blood Institute (P01HL-071064)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Porphyrin and Phthalocyanine Chemistry
- Keywords
- methemoglobin, nitric oxide, nitrite, nitrate, distal heme pocket, glass matrix, S-nitrosoglutathione, heme conformation
- MeSH terms
- Desiccation, Gases, Glass, Hydrogen-Ion Concentration, Methemoglobin, Metmyoglobin, Nitrates, Nitric Oxide, Nitrites, Oxidation-Reduction, Spectrometry, Fluorescence, Fluorescein
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
