Mechanism of Hypochlorous Acid-Mediated Heme Destruction and Free Iron Release
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Here, we show that hypochlorous acid (HOCl), a potent neutrophil-generated oxidant, can mediate destruction of free heme (Ht) and the heme precursor, protoporphyrin IX (PPIX). Ht displays a broad Soret absorbance peak centered at 365 and 394 nm, indicative of the presence of monomer and μ-oxo-dimer. Oxidation of Ht by HOCl was accompanied by a marked decrease in the Soret absorption peak and release of free iron. Kinetic measurements showed that the Ht-HOCl reaction was triphasic. The first two phases were HOCl concentration dependent and attributable to HOCl binding to the monomeric and dimeric forms. The third phase was HOCl concentration independent and attributed to Ht destruction with the release of free iron. HPLC and LC-ESI-MS analyses of the Ht-HOCl reaction revealed the formation of a number of degradation products, resulting from the cleavage or modification of one or more carbon-methene bridges of the porphyrin ring. Similar studies with PPIX showed that HOCl also mediated tetrapyrrole ring destruction. Collectively, this work demonstrates the ability of HOCl to modulate destruction of heme, through a process that occurs independent of the iron molecule that resides in the porphyrin center. This phenomenon may play a role in HOCl-mediated oxidative injury in pathological conditions.
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Hydroxyl radical formation may occur downstream of either Fe(II)-dependent Fenton chemistry, scenarios observable under conditions of MPO-facilitated heme degradation as a consequence of excess HOCl formation or pathological elevation of labile iron.
“hydroxyl radical formation may occur downstream of either Fe(II)-dependent Fenton chemistry, scenarios observable under conditions of MPO-facilitated heme degradation as a consequence of excess HOCl formation or pathological elevation of labile iron (65–67).”
From Hypochlorous Acid: From Innate Immune Factor and Environmental Toxicant to Chemopreventive Agent Targeting Solar UV-Induced Skin Cancer (2022) · cites this paper as [65]
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Interface N-glycans drive myeloperoxidase dimerization in vitro
Leitgeb, U., Guo, Y., Emde, T., Ruocco, V., Simak, T., Zdenkovic, E., Furtmüller, P. G., Borek, D., Nauseef, W. M., Oostenbrink, C., et al. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.154499
- Authors
- Maitra, D., Byun, J., Andreana, P. R., Abdulhamid, I., Saed, G. M., Diamond, M. P., Pennathur, S., & Abu-Soud, H. M.
- Affiliations
- Wayne State University (US)
- University of Michigan (US)
- ORCID
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2011-07
- Volume
- 51
- Issue
- 2
- Pages
- 364-373
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC3378337
- OpenAlex
- W2080983244
- Cited by
- 51
- References
- 50
- Citations by year
- 2026: 3 · 2025: 4 · 2023: 2 · 2022: 5 · 2021: 1 · 2020: 4 · 2019: 1 · 2018: 4 · 2017: 2 · 2016: 4 · 2015: 4 · 2014: 2 · 2013: 4 · 2012: 7
- FWCI
- 2.51
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (R01HL094230, R01HL066367)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK089503, P30DK089503)
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Porphyrin and Phthalocyanine Chemistry
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Keywords
- hypochlorous acid, heme oxidation, protoporphyrin IX, heme degradation products, oxidative damage, reaction kinetics, Soret absorption
- MeSH terms
- Chromatography, High Pressure Liquid, Heme, Hypochlorous Acid, Iron, Spectrometry, Mass, Electrospray Ionization
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