Evidence map›Paper›PMID 23775069›Full record

ArticleThe Journal of biological chemistry2013

Generating S-nitrosothiols from hemoglobin: mechanisms, conformational dependence, and physiological relevance.

Camille J Roche, Maria B Cassera, David Dantsker, Rhoda Elison Hirsch, Joel M Friedman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. The chemical biology of dinitrogen trioxide.Redox biochemistry and chemistry · 2024
    Article
  3. Review
  4. Review
  5. βCysteine 93 in human hemoglobin: a gateway to oxidative stability in health and disease.Laboratory investigation; a journal of technical methods and pathology · 2021
    Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Bio-inspired nanomedicine strategies for artificial blood components.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2017
    Review
  12. Review
  13. Article
  14. A mathematical model for the role of NNitric oxide : biology and chemistry · 2016
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Camille J RocheDepartment of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Maria B Cassera
David Dantsker
Rhoda Elison Hirsch
Joel M Friedman
Albert Einstein College of Medicine · US

Funding

New Paradigms in the Design of Blood SubstitutesP01HL071064 · NHLBI · YESHIVA UNIVERSITY · PI FRIEDMAN, JOEL M · 2002 to 2006
$11.8M
Recombinant HbAp Production for In Vivo Toxicity StudiesP01HL110900 · NHLBI · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI ALAYASH, ABDU I. · 2012 to 2016
$10.6M
Production of Bioactive NO: Origin of Hemoglobin E Associated PathophysiologyR21HL106421 · NHLBI · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI FRIEDMAN, JOEL M, HIRSCH, RHODA · 2011 to 2012
$457k
MASS SPECTROMETER SYSTEM: OBESITYS10RR019352 · NCRR · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI ANGELETTI, RUTH HOGUE · 2004 to 2004
$379k
NCRR NIH HHS S10 RR019352NHLBI NIH HHS P01 HL071064NHLBI NIH HHS P01-HL071064NHLBI NIH HHS P01 HL110900NHLBI NIH HHS P01-HL110900-01A1NHLBI NIH HHS R21 HL106421NHLBI NIH HHS R21HL 106421
6 · The paper itself

Abstract

In vitro, ferrous deoxy-hemes in hemoglobin (Hb) react with nitrite to generate nitric oxide (NO) through a nitrite reductase reaction. In vivo studies indicate Hb with nitrite can be a source of NO bioactivity. The nitrite reductase reaction does not appear to account fully for this activity because free NO is short lived especially within the red blood cell. Thus, the exporting of NO bioactivity both out of the RBC and over a large distance requires an additional mechanism. A nitrite anhydrase (NA) reaction in which N2O3, a potent S-nitrosating agent, is produced through the reaction of NO with ferric heme-bound nitrite has been proposed (Basu, S., Grubina, R., Huang, J., Conradie, J., Huang, Z., Jeffers, A., Jiang, A., He, X., Azarov, I., Seibert, R., Mehta, A., Patel, R., King, S. B., Hogg, N., Ghosh, A., Gladwin, M. T., and Kim-Shapiro, D. B. (2007) Nat. Chem. Biol. 3, 785-794) as a possible mechanism. Legitimate concerns, including physiological relevance and the nature of the mechanism, have been raised concerning the NA reaction. This study addresses these concerns demonstrating NO and nitrite with ferric hemes under near physiological conditions yield an intermediate having the properties of the purported NA heme-bound N2O3 intermediate. The results indicate that ferric heme sites, traditionally viewed as a source of potential toxicity, can be functionally significant, especially for partially oxygenated/partially met-R state Hb that arises from the NO dioxygenation reaction. In the presence of low levels of nitrite and either NO or a suitable reductant such as L-cysteine, these ferric heme sites can function as a generator for the formation of S-nitrosothiols such as S-nitrosoglutathione and, as such, should be considered as a source of RBC-derived and exportable bioactive NO.

Indexed as

Chromatography, High Pressure LiquidFluorescenceHemoglobinsHumansMass SpectrometryMolecular ConformationS-NitrosothiolsHemoglobinsS-NitrosothiolsAllosteric RegulationGlutathioneHemoglobinNitric OxideRedox Regulation

Identifiers

PMID23775069
PMCPMC3829331
OpenAlexW2087128374

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.