Evidence map›Paper›PMID 21549834›Full record

ArticleFree radical biology & medicine2011

Reaction of hemoglobin with HOCl: mechanism of heme destruction and free iron release.

Dhiman Maitra, Jaeman Byun, Peter R Andreana, Ibrahim Abdulhamid, Michael P Diamond, Ghassan M Saed, Subramaniam Pennathur, Husam M Abu-Soud

Abstract read
In one paragraph

Article in Free radical biology & medicine, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 85 citations in OpenAlex.

  1. Review
  2. Heme-mediated selection of encapsulatedEmerging microbes & infections · 2025
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  4. International journal of molecular sciences · 2024
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  5. Oxidation of hemoproteins byMicrobiology spectrum · 2024
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  7. Article
  8. Article
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  14. Article
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  16. Article
  17. Linoleic acid induces red blood cells and hemoglobin damage via oxidative mechanism.International journal of clinical and experimental pathology · 2015
    Article
  18. Article
  19. Article
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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

8 authors at 3 institutions in 1 country.

Dhiman MaitraDepartment of Obstetrics and Gynecology, The C.S. Mott Center for Human Growth and Development, Wayne State University School of Medicine, Detroit, MI 48201, USA.
Jaeman Byun
Peter R Andreana
Ibrahim Abdulhamid
Michael P Diamond
Ghassan M Saed
Subramaniam Pennathur
Husam M Abu-Soud
Wayne State University · USUniversity of Michigan–Ann Arbor · USChildren's Hospital of Michigan · US

Funding

Pilot and Feasibility (P and F) ProgramP30DK089503 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Joyce Lee · 2010 to 2026
$20.3M
Regulation of Myeloperoxidase Catalysis by Nitric OxideR01HL066367 · NHLBI · WAYNE STATE UNIVERSITY · PI ABU-SOUD, HUSAM M · 2001 to 2004
$1.2M
NHLBI NIH HHS R01 HL066367NIDDK NIH HHS DK089503NIDDK NIH HHS P30 DK089503
6 · The paper itself

Abstract

Hypochlorous acid (HOCl) is generated by myeloperoxidase using chloride and hydrogen peroxide as substrates. HOCl and its conjugate base (OCl(-)) bind to the heme moiety of hemoglobin (Hb) and generate a transient ferric species whose formation and decay kinetics indicate it can participate in protein aggregation and heme destruction along with subsequent free iron release. The oxidation of the Hb heme moiety by OCl(-) was accompanied by marked heme destruction as judged by the decrease in and subsequent flattening of the Soret absorbance peak at 405 nm. HOCl-mediated Hb heme depletion was confirmed by HPLC analysis and in-gel heme staining. Exposure of Hb to increasing concentrations of HOCl produced a number of porphyrin degradation products resulting from oxidative cleavage of one or more of the carbon-methene bridges of the tetrapyrrole ring, as identified by their characteristic HPLC fluorescence and LC-MS. A nonreducing denaturing SDS-PAGE showed several degrees of protein aggregation. Similarly, porphyrin degradation products were identified after exposure of red blood cells to increasing concentrations of HOCl, indicating biological relevance of this finding. This work provides a direct link between Hb heme destruction and subsequent free iron accumulation, as occurs under inflammatory conditions where HOCl is formed in substantial amounts.

Indexed as

Chromatography, High Pressure LiquidElectrophoresis, Polyacrylamide GelHemeHemoglobinsHypochlorous AcidIronMass SpectrometrySpectrometry, FluorescenceHemeHemoglobinsHypochlorous AcidIron

Identifiers

PMID21549834
PMCPMC3863628
OpenAlexW2044474988

What OpenQuestion holds

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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.