Evidence map›Paper›PMID 22493289›Full record

ArticleThe Journal of biological chemistry2012

Low NO concentration dependence of reductive nitrosylation reaction of hemoglobin.

Jesús Tejero, Swati Basu, Christine Helms, Neil Hogg, S Bruce King, Daniel B Kim-Shapiro, Mark T Gladwin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

28 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Cytochrome bFree radical biology & medicine · 2026
    Article
  4. Article
  5. Article
  6. The chemical biology of dinitrogen trioxide.Redox biochemistry and chemistry · 2024
    Article
  7. Mechanistic insights into cell-free hemoglobin-induced injury during septic shock.American journal of physiology. Heart and circulatory physiology · 2021
    Article
  8. Article
  9. Article
  10. Regulation of erythrocyte NaThe Journal of biological chemistry · 2019
    Article
  11. Article
  12. Review
  13. A mathematical model for the role of NNitric oxide : biology and chemistry · 2016
    Article
  14. Reactions between nitrosopersulfide and heme proteins.Free radical biology & medicine · 2016
    Article
  15. Can erythrocytes release biologically active NO?Cell communication and signaling : CCS · 2016
    Article
  16. Article
  17. Article
  18. Pitfalls in measuring NO bioavailability using NOx.Nitric oxide : biology and chemistry · 2015
    Article
  19. Article
  20. 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

7 authors at 3 institutions in 1 country.

Jesús TejeroVascular Medicine Institute, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, USA.
Swati Basu
Christine Helms
Neil Hogg
S Bruce King
Daniel B Kim-Shapiro
Mark T Gladwin
Wake Forest University · USMedical College of Wisconsin · USUniversity of Pittsburgh · US

Funding

Storage Lesion in Banked Blood Due to Disruption of Nitric Oxide HomeostasisR01HL098032 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Mark T Gladwin · 2009 to 2026
$12.5M
Effects of Nitric Oxide in Sickle Cell BloodR37HL058091 · NHLBI · WAKE FOREST UNIVERSITY · PI KIM-SHAPIRO, DANIEL B · 2007 to 2016
$3.5M
Effects of Nitric Oxide in Sickle Cell BloodR01HL058091 · NHLBI · WAKE FOREST UNIVERSITY · PI KIM-SHAPIRO, DANIEL B · 2002 to 2006
$1.6M
Myoglobin as a Nitrite Reductase that Regulates Hypoxic Cardiac NO SignalingR01HL096973 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GLADWIN, MARK T, SHIVA, SRUTI · 2010 to 2013
$1.5M
Dietary nitrate activation of PPARgamma improves insulin sensitivityRC1DK085852 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI FREEMAN, BRUCE ALAN, GLADWIN, MARK T · 2009 to 2010
$999k
MECHANISM AND KINETICS OF SICKLE CELL HEMOGLOBINR29HL058091 · NHLBI · WAKE FOREST UNIVERSITY · PI KIM-SHAPIRO, DANIEL B · 1998 to 2002
$260k
NHLBI NIH HHS HL058091NHLBI NIH HHS HL096973NHLBI NIH HHS HL098032NHLBI NIH HHS R01 HL058091NHLBI NIH HHS R01 HL096973NHLBI NIH HHS R01 HL098032NHLBI NIH HHS R29 HL058091NHLBI NIH HHS R37 HL058091NIDDK NIH HHS DK085852NIDDK NIH HHS RC1 DK085852
6 · The paper itself

Abstract

The reductive nitrosylation of ferric (met)hemoglobin is of considerable interest and remains incompletely explained. We have previously observed that at low NO concentrations the reaction with tetrameric hemoglobin occurs with an observed rate constant that is at least 5 times faster than that observed at higher concentrations. This was ascribed to a faster reaction of NO with a methemoglobin-nitrite complex. We now report detailed studies of this reaction of low NO with methemoglobin. Nitric oxide paradoxically reacts with ferric hemoglobin with faster observed rate constants at the lower NO concentration in a manner that is not affected by changes in nitrite concentration, suggesting that it is not a competition between NO and nitrite, as we previously hypothesized. By evaluation of the fast reaction in the presence of allosteric effectors and isolated β- and α-chains of hemoglobin, it appears that NO reacts with a subpopulation of β-subunit ferric hemes whose population is influenced by quaternary state, redox potential, and hemoglobin dimerization. To further characterize the role of nitrite, we developed a system that oxidizes nitrite to nitrate to eliminate nitrite contamination. Removal of nitrite does not alter reaction kinetics, but modulates reaction products, with a decrease in the formation of S-nitrosothiols. These results are consistent with the formation of NO(2)/N(2)O(3) in the presence of nitrite. The observed fast reductive nitrosylation observed at low NO concentrations may function to preserve NO bioactivity via primary oxidation of NO to form nitrite or in the presence of nitrite to form N(2)O(3) and S-nitrosothiols.

Indexed as

Allosteric RegulationHemoglobinsHumansHydrogen-Ion ConcentrationNitric OxideNitroso CompoundsOxidation-ReductionProtein BindingHemoglobinsNitric OxideNitroso Compounds

Identifiers

PMID22493289
PMCPMC3365727
OpenAlexW1999416857

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.