Myeloperoxidase Acts as a Source of Free Iron During Steady-State Catalysis by a Feedback Inhibitory Pathway
Open accessAbstract
Myeloperoxidase (MPO) is a heme-containing enzyme that generates hypochlorous acid (HOCl) from chloride (Cl(-)) and hydrogen peroxide (H₂O₂). It is implicated in the pathology of several chronic inflammatory conditions such as cardiovascular and pulmonary diseases and cancer. Recently we have shown that HOCl can destroy the heme prosthetic group of hemoproteins. Here, we investigated whether the HOCl formed during steady-state catalysis is able to destroy the MPO heme moiety and thereby function as a major source of free iron. UV-visible spectra and H₂O₂-specific electrode measurements recorded during steady-state HOCl synthesis by MPO showed that the degree of MPO heme destruction increased after multiple additions of H₂O₂ (10 µM), precluding the enzyme from functioning at maximum activity (80-90% inhibition). MPO heme destruction occurred only in the presence of Cl(-). Stopped-flow measurements revealed that the HOCl-mediated MPO heme destruction was complex and occurred through transient ferric species whose formation and decay kinetics indicated it participates in heme destruction along with subsequent free iron release. MPO heme depletion was confirmed by the buildup of free iron utilizing the ferrozine assay. Hypochlorous acid, once generated, first equilibrates in the solution as a whole before binding to the heme iron and initiating heme destruction. Eliminating HOCl from the MPO milieu by scavenging HOCl, destabilizing the MPO-Compound I-Cl complex that could be formed during catalysis, and/or inhibiting MPO catalytic activity partially or completely protects MPO from HOCl insults. Collectively, this study elucidates the bidirectional relationship between MPO and HOCl, which highlights the potential role of MPO as a source of free iron.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
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 [66]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Myeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282 · see citing works
Inside the Neutrophil Phagosome: Oxidants, Myeloperoxidase, and Bacterial Killing
Hampton, M. B., Kettle, A. J., & Winterbourn, C. C. (1998) · Blood · doi:10.1182/blood.v92.9.3007.421k47_3007_3017 · Cited by 1,640 · see citing works
Daugherty, A., Dunn, J. L., Rateri, D. L., & Heinecke, J. W. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117342 · Cited by 1,269 · see citing works
Free heme toxicity and its detoxification systems in human
Kumar, S., & Bandyopadhyay, U. (2005) · Toxicology Letters · doi:10.1016/j.toxlet.2005.03.004 · Cited by 852 · see citing works
Carter, P. M. (1971) · Analytical Biochemistry · doi:10.1016/0003-2697(71)90405-2 · Cited by 787 · see citing works
Iron and metal regulation in bacteria
Hantke, K. (2001) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(00)00184-3 · Cited by 755 · see citing works
Myeloperoxidase: a front-line defender against phagocytosed microorganisms
Klebanoff, S. J., Kettle, A. J., Rosen, H., Winterbourn, C. C., & Nauseef, W. M. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0712349 · Cited by 679 · see citing works
Myeloperoxidase-generated oxidants and atherosclerosis
Podrez, E. A., Abu‐Soud, H. M., & Hazen, S. L. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00229-x · Cited by 605 · see citing works
Self-citationMammalian Heme Peroxidases: From Molecular Mechanisms to Health Implications
Davies, M. J., Hawkins, C. L., Pattison, D. I., & Rees, M. D. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1927 · Cited by 556 · see citing works
Molecular and cellular mechanisms of iron homeostasis and toxicity in mammalian cells
Crichton, R. R., Wilmet, S., Legssyer, R., & Ward, R. J. (2002) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(02)00461-0 · Cited by 494 · see citing works
Redox Reactions and Microbial Killing in the Neutrophil Phagosome
Winterbourn, C. C., & Kettle, A. J. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4827 · Cited by 468 · see citing works
Nitric Oxide Is a Physiological Substrate for Mammalian Peroxidases
Abu‐Soud, H. M., & Hazen, S. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.48.37524 · Cited by 398 · see citing works
Self-citationYamaguchi, K., Mandai, M., Toyokuni, S., Hamanishi, J., Higuchi, T., Takakura, K., & Fujii, S. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-1614 · Cited by 324 · see citing works
Eosinophil peroxidase nitrates protein tyrosyl residues
Wu, W., Chen, Y., & Hazen, S. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25933 · Cited by 265 · see citing works
Malle, E., Waeg, G., Schreiber, R., Gröne, E. F., Sattler, W., & Gröne, H. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01498.x · Cited by 245 · see citing works
Wang, L., Bassiri, M., Najafi, R., Najafi, K. H. B. R. M. A. N. R., Yang, J., Khosrovi, B., Hwong, W., Barati, E., Belisle, B., Celeri, C., et al. (2007) · PubMed Central · Cited by 237 · see citing works
Mechanism of Reaction of Myeloperoxidase with Nitrite
Burner, U., Furtmüller, P. G., Kettle, A. J., Koppenol, W. H., & Obinger, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000181200 · Cited by 220 · see citing works
Myeloperoxidase, modified lipoproteins, and atherogenesis
Nicholls, S. J., & Hazen, S. L. (2008) · Journal of Lipid Research · doi:10.1194/jlr.r800086-jlr200 · Cited by 209 · see citing works
Potential involvement of iron in the pathogenesis of peritoneal endometriosis
Defrere, S., Lousse, J. C., Gonzalez-Ramos, R., Colette, S., Donnez, J., & Van Langendonckt, A. (2008) · Molecular Human Reproduction · doi:10.1093/molehr/gan033 · Cited by 204 · see citing works
Nitric Oxide Modulates the Catalytic Activity of Myeloperoxidase
Abu‐Soud, H. M., & Hazen, S. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5425 · Cited by 195 · see citing works
Self-citationReactive oxidants and myeloperoxidase and their involvement in neutrophil extracellular traps
Parker, H. A., & Winterbourn, C. C. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00424 · Cited by 175 · see citing works
Chloroperoxidase halogenation reactions. Chemical versus enzymic halogenating intermediates.
Libby, R. D., Thomas, J. A., Kaiser, L. W., & Hager, L. P. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34630-1 · Cited by 175 · see citing works
Emerging role of myeloperoxidase and oxidant stress markers in cardiovascular risk assessment
Brennan, M., & Hazen, S. L. (2003) · Current Opinion in Lipidology · doi:10.1097/00041433-200308000-00003 · Cited by 153 · see citing works
Mechanism of reaction of myeloperoxidase with hydrogen peroxide and chloride ion
Furtmüller, P. G., Obinger, C., Hsuanyu, Y., & Dunford, H. B. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01491.x · Cited by 124 · see citing works
Melatonin Is a Potent Inhibitor for Myeloperoxidase
Galijašević, S., Abdulhamid, I. B., & Abu‐Soud, H. M. (2008) · Biochemistry · doi:10.1021/bi702016q · Cited by 110 · see citing works
Self-citationPotent antioxidative activity of lycopene: A potential role in scavenging hypochlorous acid
Pennathur, S., Maitra, D., Byun, J., Sliskovic, I., Abdulhamid, I. B., Saed, G. M., Diamond, M. P., & Abu‐Soud, H. M. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.04.003 · Cited by 110 · see citing works
Self-citationAndrews, P. C., & Krinsky, N. I. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33436-7 · Cited by 107 · see citing works
Molecular pathogenesis of iron overload
Trinder, D., Fox, C., Vautier, G., & Olynyk, J. K. (2002) · Gut · doi:10.1136/gut.51.2.290 · Cited by 93 · see citing works
Redox properties of myeloperoxidase
Arnhold, J., Furtmüller, P. G., & Obinger, C. (2003) · Redox Report · doi:10.1179/135100003225002664 · Cited by 91 · see citing works
Ong, W.-Y., & Halliwell, B. B. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.005 · Cited by 89 · see citing works
Characterization of non-covalent oligomers of proteins treated with hypochlorous acid
Chapman, A., Winterbourn, C. C., Brennan, S. O., Jordan, T. W., & Kettle, A. J. (2003) · Biochemical Journal · doi:10.1042/bj20030685 · Cited by 89 · see citing works
Rakita, R. M., Michel, B. R., & Rosen, H. (1990) · Biochemistry · doi:10.1021/bi00456a033 · Cited by 88 · see citing works
Reaction of hemoglobin with HOCl: Mechanism of heme destruction and free iron release
Maitra, D., Byun, J., Andreana, P. R., Abdulhamid, I. B., Diamond, M. P., Saed, G. M., Pennathur, S., & Abu‐Soud, H. M. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.011 · Cited by 84 · see citing works
Self-citationOxidative Stress and “Senescent” Fibroblasts in Non-Healing Wounds as Potential Therapeutic Targets
Clark, R. A. F. (2008) · Journal of Investigative Dermatology · doi:10.1038/jid.2008.257 · Cited by 83 · see citing works
Abu‐Soud, H. M., Khassawneh, M. Y., Sohn, J., Murray, P. A., Haxhiu, M. A., & Hazen, S. L. (2001) · Biochemistry · doi:10.1021/bi011206v · Cited by 81 · see citing works
Self-citationBactericidal potency of hydroxyl radical in physiological environments
Wolcott, R. G., Franks, B. S., Hannum, D. M., & Hurst, J. K. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36942-9 · Cited by 64 · see citing works
Menegazzi, R., Busetto, S., Dri, P., Cramer, R., & Patriarca, P. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.135.2.511 · Cited by 64 · see citing works
Samuni, A., & Czapski, G. (1978) · Radiation Research · doi:10.2307/3574810 · Cited by 60 · see citing works
Thiocyanate Modulates the Catalytic Activity of Mammalian Peroxidases
Tahboub, Y. R., Galijašević, S., Diamond, M. P., & Abu‐Soud, H. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503027200 · Cited by 58 · see citing works
Self-citationMechanism of Hypochlorous Acid-Mediated Heme Destruction and Free Iron Release
Maitra, D., Byun, J., Andreana, P. R., Abdulhamid, I., Saed, G. M., Diamond, M. P., Pennathur, S., & Abu-Soud, H. M. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.03.040 · Cited by 51 · see citing works
Self-citationThe reaction of HOCl and cyanocobalamin: Corrin destruction and the liberation of cyanogen chloride
Abu‐Soud, H. M., Maitra, D., Byun, J., Souza, C. E. A., Banerjee, J., Saed, G. M., Diamond, M. P., Andreana, P. R., & Pennathur, S. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.496 · Cited by 47 · see citing works
Self-citationThe reactivity of myeloperoxidase compound I formed with hypochlorous acid
Furtmüller, P. G., Burner, U., Jantschko, W., Regelsberger, G., & Obinger, C. (2000) · Redox Report · doi:10.1179/135100000101535717 · Cited by 46 · see citing works
Fletcher, N. M., Jiang, Z., Ali‐Fehmi, R., Levin, N. K., Belotte, J., Tainsky, M. A., Diamond, M. P., Abu‐Soud, H. M., & Saed, G. M. (2012) · Cancer Biomarkers · doi:10.3233/cbm-2012-0255 · Cited by 43 · see citing works
Self-citationReaction of myeloperoxidase with its product HOCI
Floris, R., & Wever, R. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17097.x · Cited by 43 · see citing works
Souza, C. E. A., Maitra, D., Saed, G. M., Diamond, M. P., Moura, A. A., Pennathur, S., & Abu‐Soud, H. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0027641 · Cited by 43 · see citing works
Self-citationInterrogation of Heme Pocket Environment of Mammalian Peroxidases with Diatomic Ligands
Abu‐Soud, H. M., & Hazen, S. L. (2001) · Biochemistry · doi:10.1021/bi010478v · Cited by 42 · see citing works
Self-citationFittschen, C., & Henson, P. M. (1994) · Journal of Clinical Investigation · doi:10.1172/jci116952 · Cited by 42 · see citing works
Potential role of tryptophan and chloride in the inhibition of human myeloperoxidase
Galijašević, S., Abdulhamid, I. B., & Abu‐Soud, H. M. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.01.003 · Cited by 39 · see citing works
Self-citationChau, L. (2000) · PubMed · Cited by 37 · see citing works
Modified Lipoproteins and Atherogenesis
Berliner, J. A., Territo, M., Amdalibi, A., Navab, M., Liao, F., Cushing, S. D., Imes, S., Kim, J., Lenten, B. J. V., Lusis, A. J., et al. (1992) · The Argenteuil symposia · doi:10.1007/978-1-4471-1909-8_7 · Cited by 37 · see citing works
Analysis of the mechanism by which tryptophan analogs inhibit human myeloperoxidase
Sliskovic, I., Abdulhamid, I. B., Sharma, M., & Abu‐Soud, H. M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.07.007 · Cited by 36 · see citing works
Self-citationBritigan, B. E. (1996) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(96)00014-1 · Cited by 36 · see citing works
Myeloperoxidase interaction with peroxynitrite: chloride deficiency and heme depletion
Galijašević, S., Maitra, D., Lu, T., Sliskovic, I., Abdulhamid, I. B., & Abu‐Soud, H. M. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.017 · Cited by 34 · see citing works
Self-citationMyeloperoxidase-catalyzed taurine chlorination: Initial versus equilibrium rate
Ramos, D. R., García, M. V., Canle, M., Santaballa, J. A., Furtmüller, P. G., & Obinger, C. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.07.024 · Cited by 32 · see citing works
Vivekanandan‐Giri, A., Wang, J. H., Byun, J., & Pennathur, S. (2008) · Reviews in Endocrine and Metabolic Disorders · doi:10.1007/s11154-008-9093-1 · Cited by 30 · see citing works
Self-citationProteasa, G., Tahboub, Y. R., Galijašević, S., Raushel, F. M., & Abu‐Soud, H. M. (2006) · Biochemistry · doi:10.1021/bi0609725 · Cited by 27 · see citing works
Self-citationSpectral and kinetic evidence for reaction of superoxide with compound I of myeloperoxidase
Kettle, A. J., Maroz, A., Woodroffe, G., Winterbourn, C. C., & Anderson, R. F. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.09.019 · Cited by 26 · see citing works
Maitra, D., Abdulhamid, I. B., Diamond, M. P., Saed, G. M., & Abu‐Soud, H. M. (2012) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2012.00988.x · Cited by 25 · see citing works
Self-citationReactions of hypochlorite with catalase
Mashino, T., & Fridovich, I. (1988) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(88)90298-1 · Cited by 20 · see citing works
Abu‐Soud, H. M., Raushel, F. M., & Hazen, S. L. (2004) · Biochemistry · doi:10.1021/bi049541h · Cited by 17 · see citing works
Self-citationProperties of peroxidase from chewing stick miswak
Mohamed, S. A. (2012) · African Journal of Pharmacy and Pharmacology · doi:10.5897/ajpp12.015 · Cited by 13 · see citing works
Flagged first, then by citations
Research works printed but not linked: 2
- [45]Floris R Wever R Reaction of myeloperoxidase with its product HOCl Eur J Biochem 207 697 702 1992 1321719
- [49]Chau LY Iron and atherosclerosis Proc Natl Sci Counc, Repub China, Part B: Life Sci 24 151 155 2000 11087066
Cited by
Sorted by citations
Myeloperoxidase: Bridging the gap in neurodegeneration
Ray, R. S., & Katyal, A. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.06.031 · Cited by 114 · see citing works
Myeloperoxidase and Neurological Disorder: A Crosstalk
Pravalika, K., Sarmah, D., Kaur, H., Wanve, M., Saraf, J., Kalia, K., Borah, A., Yavagal, D. R., Dave, K. R., & Bhattacharya, P. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00462 · Cited by 91 · see citing works
Goud, P. T., Bai, D., & Abu-Soud, H. M. (2021) · International Journal of Biological Sciences · doi:10.7150/ijbs.51811 · Cited by 88 · see citing works
Self-citationShaeib, F., Khan, S., Ali, I., Thakur, M., Saed, G. M., Dai, J., Awonuga, A. O., Banerjee, J., & Abu‐Soud, H. M. (2015) · Reproductive Sciences · doi:10.1177/1933719115607993 · Cited by 79 · see citing works
Self-citationStamp, L. K., Turner, R., Khalilova, I. S., Zhang, M., Drake, J. M., Forbes, L. V., & Kettle, A. J. (2014) · Lara D. Veeken · doi:10.1093/rheumatology/keu218 · Cited by 56 · see citing works
Yang, H., Zhou, W., Gu, C., Meng, Y., Shao, J., Li, D., & Li, M. (2018) · American Journal of Reproductive Immunology · doi:10.1111/aji.12839 · Cited by 56 · see citing works
Yeoh, B. S., Olvera, R. A., Singh, V., Xiao, X., Kennett, M. J., Joe, B., Lambert, J. D., & Vijay–Kumar, M. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2015.12.004 · Cited by 49 · see citing works
Melatonin interferes with COVID-19 at several distinct ROS-related steps
Camp, O. G., Bai, D., Gonullu, D. C., Nayak, N., & Abu‐Soud, H. M. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111546 · Cited by 43 · see citing works
Self-citationNon-Canonical Functions of Myeloperoxidase in Immune Regulation, Tissue Inflammation and Cancer
Lockhart, J., & Sumagin, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012250 · Cited by 39 · see citing works
The Impact of Myeloperoxidase and Activated Macrophages on Metaphase II Mouse Oocyte Quality
Shaeib, F., Khan, S., Thakur, M., Kohan‐Ghadr, H., Drewlo, S., Saed, G. M., Pennathur, S., & Abu‐Soud, H. M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0151160 · Cited by 39 · see citing works
Self-citationNeutrophil activation in response to monomeric myeloperoxidase
Gorudko, I. V., Grigorieva, D. V., Av, S., Shamova, E. V., Kostevich, V. A., Kudryavtsev, I. V., Syromiatnikova, E. D., Vasilyev, V. B., Cherenkevich, S. N., & Panasenko, O. M. (2018) · Biochemistry and Cell Biology · doi:10.1139/bcb-2017-0290 · Cited by 38 · see citing works
Snell, J. A., Jandova, J., & Wondrak, G. T. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.887220 · Cited by 37 · see citing works
Gorudko, I. V., Av, S., Shamova, E. V., Grigorieva, D. V., Mironova, E. V., Kudryavtsev, I. V., Гусев, С. А., Gusev, A. A., Chekanov, A. V., Vasilyev, V. B., et al. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.12.007 · Cited by 35 · see citing works
Tolmacheva, A. S., & Nevinsky, G. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073898 · Cited by 32 · see citing works
Abarikwu, S. O., Oruitemeka, S., Uwadileke, I. A., Omeodu, S. I., Okoye, N. F., Mgbudom‐Okah, C. J., & Ohanador, R. (2018) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2018.04.011 · Cited by 31 · see citing works
Jeelani, R., Maitra, D., Chatzicharalampous, C., Najeemuddin, S., Morris, R. T., & Abu‐Soud, H. M. (2017) · Journal of Pineal Research · doi:10.1111/jpi.12463 · Cited by 28 · see citing works
Self-citationCatalase prevents myeloperoxidase self-destruction in response to oxidative stress
Ali, I., Khan, S., Chatzicharalampous, C., Bai, D., & Abu‐Soud, H. M. (2019) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2019.110706 · Cited by 29 · see citing works
Self-citationZhang, P., Wei, L., Jiang, Q., Gai, S., Zhou, Z., Bian, J., Zhang, Y., Han, W., Shu, W., & He, Y. (2023) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2023.107051 · Cited by 28 · see citing works
Xiao, X., Yeoh, B. S., Saha, P., Olvera, R. A., Singh, V., & Vijay–Kumar, M. (2016) · BioMetals · doi:10.1007/s10534-016-9925-5 · Cited by 28 · see citing works
Hypochlorous acid reversibly inhibits caspase-3: a potential regulator of apoptosis
Jeelani, R., Chatzicharalampous, C., Kohan‐Ghadr, H., Bai, D., Morris, R. T., Sliskovic, I., Awonuga, A. O., & Abu‐Soud, H. M. (2020) · Free Radical Research · doi:10.1080/10715762.2019.1694675 · Cited by 27 · see citing works
Self-citationMechanism of reaction of chlorite with mammalian heme peroxidases
Jakopitsch, C., Pirker, K. F., Flemmig, J., Hofbauer, S., Schlorke, D., Furtmüller, P. G., Arnhold, J., & Obinger, C. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.02.010 · Cited by 27 · see citing works
Ye, J., Qin, Y., Liu, H., Xiong, H., Zhang, H., Shen, H., Zeng, F., Shi, C., & Zhou, Z. (2025) · ACS Nano · doi:10.1021/acsnano.4c18555 · Cited by 26 · see citing works
Diffused Intra-Oocyte Hydrogen Peroxide Activates Myeloperoxidase and Deteriorates Oocyte Quality
Khan, S., Shaeib, F., Najafi, T., Kavdia, M., Gonik, B., Saed, G. M., Goud, P. T., & Abu‐Soud, H. M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0132388 · Cited by 26 · see citing works
Self-citationWalter, L. O., Cardoso, C. C., Santos‐Pirath, Í. M., Costa, H. Z., Gartner, R., Werle, I., Mohr, E. T. B., da Rosa, J. S., Felisberto, M., Kretzer, I. F., et al. (2022) · Immunology · doi:10.1111/imm.13457 · Cited by 24 · see citing works
Hair, P. S., Sass, L. A., Krishna, N. K., & Cunnion, K. M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0170203 · Cited by 21 · see citing works
Disruption of heme-peptide covalent cross-linking in mammalian peroxidases by hypochlorous acid
Abu‐Soud, H. M., Maitra, D., Shaeib, F., Khan, S., Byun, J., Abdulhamid, I. B., Yang, Z., Saed, G. M., Diamond, M. P., Andreana, P. R., et al. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.06.018 · Cited by 20 · see citing works
Self-citationMorphine, a potential inhibitor of myeloperoxidase activity
Nyssen, P., Mouithys-Mickalad, A. A., Minguet, G., Sauvage, E., Wouters, J., Franck, T. J., & Hoebeke, M. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.07.007 · Cited by 19 · see citing works
Kinetic Studies on the Reaction between Dicyanocobinamide and Hypochlorous Acid
Maitra, D., Ali, I., Abdulridha, R. M., Shaeib, F., Khan, S., Saed, G. M., Pennathur, S., & Abu‐Soud, H. M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0110595 · Cited by 18 · see citing works
Self-citationShaeib, F., Khan, S., Ali, I., Najafi, T., Maitra, D., Abdulhamid, I. B., Saed, G. M., Pennathur, S., & Abu‐Soud, H. M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0120737 · Cited by 18 · see citing works
Self-citationMesna (2-mercaptoethane sodium sulfonate) functions as a regulator of myeloperoxidase
Jeelani, R., Jahanbakhsh, S., Kohan‐Ghadr, H., Thakur, M., Khan, S., Aldhaheri, S. R., Yang, Z., Andreana, P. R., Morris, R. T., & Abu‐Soud, H. M. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.05.019 · Cited by 18 · see citing works
Self-citationNutritional deficiencies that may predispose to long COVID
Schloss, J. V. (2023) · Inflammopharmacology · doi:10.1007/s10787-023-01183-3 · Cited by 17 · see citing works
Pullar, J., Carr, A., Bozonet, S., Rosengrave, P. C., Kettle, A. J., & Vissers, M. (2017) · Andrology · doi:10.1111/andr.12327 · Cited by 18 · see citing works
Quantitative proteomics by iTRAQ-PRM based reveals the new characterization for gout
Chen, G., Cheng, J., Yu, H., Huang, X., Bao, H. F., Qin, L., Wang, L., Song, Y., Liu, X., & Peng, A. (2021) · Proteome Science · doi:10.1186/s12953-021-00180-0 · Cited by 15 · see citing works
Pérez, L. C. C., Gutiérrez‐Sánchez, M., Wejebe, J. E. M., Rodríguez, M. H., Fragoso-Vázquez, M. J., Salazar, J. R., Correa‐Basurto, J., Martínez, I. I. P., & Rosales‐Hernández, M. C. (2017) · Arabian Journal of Chemistry · doi:10.1016/j.arabjc.2016.12.026 · Cited by 15 · see citing works
Myeloperoxidase deficiency attenuates systemic and dietary iron-induced adverse effects
Xiao, X., Saha, P., Yeoh, B. S., Hipp, J., Singh, V., & Vijay–Kumar, M. (2018) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2018.08.003 · Cited by 12 · see citing works
Enzymatic and bactericidal activity of myeloperoxidase in conditions of halogenative stress
Vakhrusheva, T. V., Grigorieva, D. V., Gorudko, I. V., Av, S., Kostevich, V. A., Лазарев, В. Н., Vasilyev, V. B., Cherenkevich, S. N., & Panasenko, O. M. (2018) · Biochemistry and Cell Biology · doi:10.1139/bcb-2017-0292 · Cited by 12 · see citing works
Hypochlorous acid inactivates myeloperoxidase inside phagocytosing neutrophils
Paumann-Page, M., Ashby, L. V., Khalilova, I. S., Magon, N. J., Hofbauer, S., Paton, L. N., Furtmüller, P. G., Obinger, C., & Kettle, A. J. (2023) · Redox Biochemistry and Chemistry · doi:10.1016/j.rbc.2023.100008 · Cited by 10 · see citing works
Coronel, P. M. V., Pereira, I. C., Basilio, D. C. L. S., Espinoça, I. T., de Souza, K. F. S., Ota, R. S. N., de Almeida, E. B., Paredes‐Gamero, E. J., Filho, D. W., Perdomo, R. T., et al. (2023) · Microbial Pathogenesis · doi:10.1016/j.micpath.2023.106339 · Cited by 11 · see citing works
Peptide Inhibitor of Complement C1 Inhibits the Peroxidase Activity of Hemoglobin and Myoglobin
Hair, P. S., Cunnion, K. M., & Krishna, N. K. (2017) · International Journal of Peptides · doi:10.1155/2017/9454583 · Cited by 11 · see citing works
Camp, O. G., Bai, D., Awonuga, A. O., Goud, P. T., & Abu‐Soud, H. M. (2022) · Nitric Oxide · doi:10.1016/j.niox.2022.04.006 · Cited by 10 · see citing works
Self-citationInternational Journal of Peptides
(2009) · International Journal of Peptides · doi:10.1155/ijpep · Cited by 10 · see citing works
Hair, P. S., Enos, A. I., Krishna, N. K., & Cunnion, K. M. (2019) · PLoS ONE · doi:10.1371/journal.pone.0226875 · Cited by 9 · see citing works
Structure-biological activity relationships of myeloperoxidase to effect on platelet activation
Gorudko, I. V., Grigorieva, D. V., Shamova, E. V., Gorbunov, N., Kokhan, A. U., Kostevich, V. A., Vasilyev, V. B., Panasenko, O. M., Khinevich, N., Bandarenka, H., et al. (2022) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2022.109353 · Cited by 8 · see citing works
Mustor, E. M., Frey, A. M., Jobson, M.-E., Chaput, D., & Shaw, L. N. (2025) · mSystems · doi:10.1128/msystems.00697-25 · Cited by 6 · see citing works
Iron and atherosclerosis: Lessons learned from rabbits relevant to human disease
Halliwell, B. B., Watt, F., & Minqin, R. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.10.383 · Cited by 6 · see citing works
Enzymatic and bactericidal activity of monomeric and dimeric forms of myeloperoxidase
Vakhrusheva, T. V., Av, S., Kostevich, V. A., Vasilyev, V. B., & Panasenko, O. M. (2018) · Biomeditsinskaya Khimiya · doi:10.18097/pbmc20186402175 · Cited by 6 · see citing works
Enzymatic and Bactericidal Activity of Monomeric and Dimeric Forms of Myeloperoxidase
Vakhrusheva, T. V., Av, S., Kostevich, V. A., Vasilyev, V. B., & Panasenko, O. M. (2018) · Biochemistry (Moscow) Supplement Series B Biomedical Chemistry · doi:10.1134/s1990750818030083 · Cited by 5 · see citing works
Shaeib, F., Khan, S., Ali, I., Banarjee, J., Saed, G. M., & Abu‐Soud, H. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.10.570 · Cited by 5 · see citing works
Self-citationBiernat, M. M., Camp, O. G., Moussa, D. N., Awonuga, A. O., & Abu‐Soud, H. M. (2025) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2025.112927 · Cited by 4 · see citing works
Self-citationCamp, O. G., Bai, D., Goud, P. T., Diamond, M. P., & Abu‐Soud, H. M. (2022) · F&S Reviews · doi:10.1016/j.xfnr.2022.02.001 · Cited by 5 · see citing works
Self-citationMyeloperoxidase in the pathogenesis of sickle cell disease
Biernat, M. M., Camp, O. G., Awonuga, A. O., Abu‐Soud, H. M., Chatzicharalampous, C., Kofinas, G., & Kofinas, J. D. (2026) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2026.110800 · Cited by 2 · see citing works
Self-citationMerakeb, M. S., Bribi, N., Ferhat, R., & Afenai, S. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.120001 · Cited by 2 · see citing works
Sun, W., Hu, C., Zhao, X. X., Tao, Z., Guo, C., Zhang, Y., Atya, S. M., Skalny, A. V., Aschner, M., Yang, B., et al. (2026) · BioMetals · doi:10.1007/s10534-026-00815-9 · Cited by 1 · see citing works
The role of oxidative stress in the pathogenesis of epithelial ovarian cancer
Fletcher, N. M. (2013)
Maitra, D., Abdulridha, R. M., Abdulhamid, I. B., Saed, G. M., & Abu‐Soud, H. M. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.269
Self-citationThe Role Of Oxidative Stress In The Pathogenesis Of Epithelial Ovarian Cancer
King, N. M. (2013) · Human Biology
The Impact Of Myeloperoxidase And Its Related Oxidants On Metaphase Ii Mouse Oocyte Quality
Shaeib, F. (2016) · Human Biology
Self-citationQuantitative Proteomics by iTRAQ-PRM based Reveals the New Characterization for Gout.Preprint
Chen, G., Cheng, J., Yu, H., Huang, X., Bao, H. F., Qin, L., Wang, L., Song, Y., Liu, X., & Peng, A. (2021) · Research Square · doi:10.21203/rs.3.rs-286084/v2
Quantitative Proteomics by iTRAQ-PRM based Reveals the New Characterization for Gout.Preprint
Chen, G., Cheng, J., Yu, H., Huang, X., Bao, H. F., Qin, L., Wang, L., Song, Y., Liu, X., & Peng, A. (2021) · Research Square · doi:10.21203/rs.3.rs-286084/v1
Chen, G., Cheng, J., Yu, H., Huang, X. S., Bao, H. F., Qin, L., Wang, L., Song, Y., Liu, X., & Peng, A. (2021) · Figshare · doi:10.6084/m9.figshare.16786812
Churashova, I. A., Av, S., Kostevich, V. A., Gorbunov, N., Baranova, T. V., Firova, E. M., Mandelshtam, M. Y., & Vasilyev, V. B. (2025) · Medical academic journal · doi:10.17816/maj636892
Abnormal DHR is not always synonymous with a diagnosis of chronic granulomatous disease
Noorsaeed, S., Alizadehfar, R., Mazer, B. D., & McCusker, C. T. (2025) · BMJ Case Reports · doi:10.1136/bcr-2025-269164
Laboratory Diagnosis of Leukemia and Lymphoma
Zadeh, M. K., Kohzadi, Z., Shams, M., Valipour, N., Varmaghani, B., Samadov, A., Qayumov, M., Safdari, S. M., Beigi, M. B. D., & Narouei, F. (2026) · Springer eBooks · doi:10.1007/978-3-032-17940-1_12
Russo, T., D’Orazio, A., & Baggiani, A. (2026) · Pathogens · doi:10.3390/pathogens15090962
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., Shaeib, F., Abdulhamid, I., Abdulridha, R. M., Saed, G. M., Diamond, M. P., Pennathur, S., & Abu-Soud, H. M.
- Affiliations
- Wayne State University (US)
- Children's Hospital of Michigan (US)
- Augusta University (US)
- University of Michigan (US)
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2013-10
- Volume
- 63
- Pages
- 90-98
- ISSN
- 0891-5849 (ISSN-L)
- PMC
- PMC3863623
- OpenAlex
- W2091924757
- Cited by
- 64
- References
- 61
- Citations by year
- 2026: 5 · 2025: 6 · 2023: 5 · 2022: 7 · 2021: 4 · 2020: 2 · 2019: 2 · 2018: 9 · 2017: 6 · 2016: 5 · 2015: 4 · 2014: 5 · 2013: 2 · 2012: 1
- FWCI
- 2.95
- 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 Institutes of Health (RO1 HL066367)
- Children’s Hospital of Michigan Foundation (R01HL094230)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Keywords
- myeloperoxidase, hypochlorous acid, free iron, heme degradation, product inhibition, hydrogen peroxide, chloride, compound I, heme iron, ferrozine assay, enzyme catalysis, iron release
- MeSH terms
- Catalysis, Chlorides, Ferrozine, Free Radicals, Heme, Humans, Hydrogen Peroxide, Hypochlorous Acid, Inflammation, Iron, Kinetics, Peroxidase, Oxidation-Reduction, Feedback, Physiological, Metabolic Networks and Pathways
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
