ArticleThe Journal of biological chemistry2009
Ibuprofen impairs allosterically peroxynitrite isomerization by ferric human serum heme-albumin.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 41 citations in OpenAlex.
- Ligand-Based Regulation of Dynamics and Reactivity of Hemoproteins.Biomolecules · 2023Review
- Unraveling the versatility of human serum albumin - A comprehensive review of its biological significance and therapeutic potential.Current research in structural biology · 2023Review
- The Balancing of Peroxynitrite Detoxification between Ferric Heme-Proteins and COAntioxidants (Basel, Switzerland) · 2022Article
- Serum Albumin: A Multifaced Enzyme.International journal of molecular sciences · 2021Review
- Ferric nitrosylated myoglobin catalyzes peroxynitrite scavenging.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Structural and functional properties of Antarctic fish cytoglobins-1: Cold-reactivity in multi-ligand reactions.Computational and structural biotechnology journal · 2020Article
- Human nitrobindin: the first example of an all-β-barrel ferric heme-protein that catalyzes peroxynitrite detoxification.FEBS open bio · 2018Article
- Peroxynitrite scavenging by Campylobacter jejuni truncated hemoglobin P.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Article
- Heme-albumin: an honorary enzyme.Cell death & disease · 2015Article
- Heme-based catalytic properties of human serum albumin.Cell death discovery · 2015Review
- Analysis of the structure and dynamics of human serum albumin.Journal of molecular modeling · 2014Article
- Article
- Nitrite-reductase and peroxynitrite isomerization activities of Methanosarcina acetivorans protoglobin.PloS one · 2014Article
- Warfarin modulates the nitrite reductase activity of ferrous human serum heme-albumin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- Isoniazid inhibits the heme-based reactivity of Mycobacterium tuberculosis truncated hemoglobin N.PloS one · 2013Article
- Evidence for pH-dependent multiple conformers in iron(II) heme-human serum albumin: spectroscopic and kinetic investigation of carbon monoxide binding.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012Article
- Isoniazid and rifampicin inhibit allosterically heme binding to albumin and peroxynitrite isomerization by heme-albumin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
Corrections and comments
- Erratum issued
Authors and funding
8 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human serum albumin (HSA) participates in heme scavenging; in turn, heme endows HSA with myoglobin-like reactivity and spectroscopic properties. Here, the allosteric effect of ibuprofen on peroxynitrite isomerization to NO(3)(-) catalyzed by ferric human serum heme-albumin (HSA-heme-Fe(III)) is reported. Data were obtained at 22.0 degrees C. HSA-heme-Fe(III) catalyzes peroxynitrite isomerization in the absence and presence of CO(2); the values of the second order catalytic rate constant (k(on)) are 4.1 x 10(5) and 4.5 x 10(5) m(-1) s(-1), respectively. Moreover, HSA-heme-Fe(III) prevents peroxynitrite-mediated nitration of free added l-tyrosine. The pH dependence of k(on) (pK(a) = 6.9) suggests that peroxynitrous acid reacts preferentially with the heme-Fe(III) atom, in the absence and presence of CO(2). The HSA-heme-Fe(III)-catalyzed isomerization of peroxynitrite has been ascribed to the reactive pentacoordinated heme-Fe(III) atom. In the absence and presence of CO(2), ibuprofen impairs dose-dependently peroxynitrite isomerization by HSA-heme-Fe(III) and facilitates the nitration of free added l-tyrosine; the value of the dissociation equilibrium constant for ibuprofen binding to HSA-heme-Fe(III) (L) ranges between 7.7 x 10(-4) and 9.7 x 10(-4) m. Under conditions where [ibuprofen] is >>L, the kinetics of HSA-heme-Fe(III)-catalyzed isomerization of peroxynitrite is superimposable to that obtained in the absence of HSA-heme-Fe(III) or in the presence of non-catalytic HSA-heme-Fe(III)-cyanide complex and HSA. Ibuprofen binding impairs allosterically peroxynitrite isomerization by HSA-heme-Fe(III), inducing the hexacoordination of the heme-Fe(III) atom. These results represent the first evidence for peroxynitrite isomerization by HSA-heme-Fe(III), highlighting the allosteric modulation of HSA-heme-Fe(III) reactivity by heterotropic interaction(s), and outlining the role of drugs in modulating HSA functions. The present results could be relevant for the drug-dependent protective role of HSA-heme-Fe(III) in vivo.
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