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Cited by 399

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Is haemoglobin a biological Fenton reagent?

Open access
Puppo, A, Halliwell, B·1988·Biochemical Journal

Abstract

The ability of oxyhaemoglobin and methaemoglobin to generate hydroxyl radicals (OH.) from H2O2 has been investigated using deoxyribose and phenylalanine as ‘detector molecules’ for OH.. An excess of H2O2 degrades methaemoglobin, releasing iron ions that react with H2O2 to form a species that appears to be OH.. Oxyhaemoglobin reacts with low concentrations of H2O2 to form a ‘reactive species’ that degrades deoxyribose but does not hydroxylate phenylalanine. This ‘reactive species’ is less amenable to scavenging by certain scavengers (salicylate, phenylalanine, arginine) than is OH., but it appears more reactive than OH. is to others (Hepes, urea). The ability of haemoglobin to generate not only this ‘reactive species’, but also OH. in the presence of H2O2 may account for the damaging effects of free haemoglobin in the brain, the eye, and at sites of inflammation.

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Metadata

Authors
Puppo, A., & Halliwell, B.
Venue
Biochemical Journal
Published
1988-01-01
Volume
249
Issue
1
Pages
185-190
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
OpenAlex
W1841695296
Cited by
399
References
2
FWCI
9.02
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Is haemoglobin a biological Fenton reagent? https://app.cochat.ai/papers/10.1042/bj2490185
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Puppo, A., & Halliwell, B. (1988). Formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Is haemoglobin a biological Fenton reagent? Biochemical Journal. https://doi.org/10.1042/bj2490185

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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