ArticleJournal of the American Chemical Society2009
Direct detection of the oxygen rebound intermediates, ferryl Mb and NO2, in the reaction of metmyoglobin with peroxynitrite.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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.
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.
Who cites it
21 citing papers in PubMed, 70 citations in OpenAlex.
- Review
- Molecular Basis for Peptide Nitration by a Novel Cytochrome P450 Enzyme in RiPP Biosynthesis.ACS catalysis · 2025Article
- Vibrational analyses of the reaction of oxymyoglobin with NO using a photolabile caged NO donor at cryogenic temperatures.Journal of inorganic biochemistry · 2024Article
- The Impact of Physical Exercise on Oxidative and Nitrosative Stress: Balancing the Benefits and Risks.Antioxidants (Basel, Switzerland) · 2024Review
- Influence of Cage Effects in Directing the Outcome of C-X Bond Forming Reactions.ACS organic & inorganic Au · 2024Review
- The Ferric-Superoxo Intermediate of the TxtE Nitration Pathway Resists Reduction, Facilitating Its Reaction with Nitric Oxide.Biochemistry · 2021Article
- Catalytic Mechanism of Aromatic Nitration by Cytochrome P450 TxtE: Involvement of a Ferric-Peroxynitrite Intermediate.Journal of the American Chemical Society · 2020Article
- Towards the understanding of the enzymatic cleavage of polyisoprene by the dihaem-dioxygenase RoxA.AMB Express · 2019Article
- Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.Chemical reviews · 2018Review
- Cross-linking of dicyclotyrosine by the cytochrome P450 enzyme CYP121 fromThe Journal of biological chemistry · 2017Article
- Beyond ferryl-mediated hydroxylation: 40 years of the rebound mechanism and C-H activation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- A Peroxynitrite Dicopper Complex: Formation via Cu-NO and Cu-OJournal of the American Chemical Society · 2016Article
- Mechanistic Insight into the Nitric Oxide Dioxygenation Reaction of Nonheme Iron(III)-Superoxo and Manganese(IV)-Peroxo Complexes.Angewandte Chemie (International ed. in English) · 2016Article
- Conversion of Aldehyde to Alkane by a Peroxoiron(III) Complex: A Functional Model for the Cyanobacterial Aldehyde-Deformylating Oxygenase.Journal of the American Chemical Society · 2015Article
- Production of dioxygen in the dark: dismutases of oxyanions.Metal ions in life sciences · 2015Review
- Involvement of ferryl in the reaction between nitrite and the oxy forms of globins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Hemoglobin: a nitric-oxide dioxygenase.Scientifica · 2012Review
- Molecular probes of the mechanism of cytochrome P450. Oxygen traps a substrate radical intermediate.Archives of biochemistry and biophysics · 2011Article
- Peroxynitrite mediates active site tyrosine nitration in manganese superoxide dismutase. Evidence of a role for the carbonate radical anion.Journal of the American Chemical Society · 2010Article
- Mechanisms of peroxynitrite interactions with heme proteins.Inorganic chemistry · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Oxygenated hemoproteins are known to react rapidly with nitric oxide (NO) to produce peroxynitrite (PN) at the heme site. This process could lead either to attenuation of the effects of NO or to nitrosative protein damage. Peroxynitrite is a powerful nitrating and oxidizing agent that has been implicated in a variety of cell injuries. Accordingly, it is important to delineate the nature and variety of reaction mechanisms of PN reactions with heme proteins. Here, we present direct evidence that ferrylMb and NO(2) are both produced during the reaction of PN and metmyoglobin (metMb). Kinetic evidence indicates that these products evolve from initial formation of a caged radical intermediate [Fe(IV)=O *NO(2)]. This caged pair reacts mainly via internal return with a rate constant k(r) to form metMb and nitrate in an oxygen rebound scenario. Detectable amounts of ferrylMb are observed by stopped-flow spectrophotometry, appearing at a rate consistent with the rate, k(obs), of heme-mediated PN decomposition. Freely diffusing NO(2), which is liberated concomitantly from the radical pair (k(e)), preferentially nitrates Tyr103 in horse heart myoglobin. The ratio of the rates of in-cage rebound and cage escape, k(r)/k(e), was found to be approximately 10 by examining the nitration yields of fluorescein, an external NO(2) trap. This rebound/escape model for the metMb/PN interaction is analogous to the behavior of alkyl hyponitrites and the well-studied geminate recombination processes of deoxymyoglobin with O(2), CO, and NO. The scenario is also similar to the stepwise events of substrate hydroxylation by cytochrome P450 and other oxygenases. It is likely, therefore, that the reaction of metMb with ONOO(-) and that of oxyMb with NO proceed through the same [Fe(IV)=O *NO(2)] caged radical intermediate and lead to similar outcomes. The results indicate that while oxyMb may reduce the concentration of intracellular NO, it would not eliminate the formation of NO(2) as a decomposition product of peroxynitrite.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.