ArticleNature communications2016
Direct visualization of a Fe(IV)-OH intermediate in a heme enzyme.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 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
49 citing papers in PubMed.
- Generation and modulation of catalytically relevant states of a dye-decolourizing peroxidase using time-resolved serial femtosecond crystallography with drop-on-chip mixing and X-ray-driven reduction.Acta crystallographica. Section D, Structural biology · 2026Article
- Can ferric-oxyl excited states explain elongated iron-oxygen bonds in heme peroxidase catalytic intermediates?Nature communications · 2026Article
- A Dynamic Gate Enables Regioselective Hydroxylation of Free Arginine by a Non-Canonical Heme Enzyme.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Solvent Channels and Electric Fields Guide Proton Delivery to the Active Site of Heme Peroxidases.Angewandte Chemie (International ed. in English) · 2025Article
- Switchable High-Valent AgJACS Au · 2025Article
- Unveiling an Ultrareduced State of Heme in Myoglobin.Journal of the American Chemical Society · 2025Article
- Review
- Current and future perspectives for structural biology at the Grenoble EPN campus: a comprehensive overview.Journal of synchrotron radiation · 2025Review
- Stabilization of the Ferryl═Oxoheme Form ofJournal of the American Chemical Society · 2025Article
- Flexible iron: disorder in the ironome brings order to protein structure and function.Frontiers in molecular biosciences · 2025Article
- Peroxidase (POD) Mimicking Activity of Different Types of Poly(ethyleneimine)-Mediated Prussian Blue Nanoparticles.Nanomaterials (Basel, Switzerland) · 2024Article
- Enhanced Reactivities of Iron(IV)-Oxo Porphyrin Species in Oxidation Reactions Promoted by Intramolecular Hydrogen-Bonding.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Correlating Structure with Spectroscopy in Ascorbate Peroxidase Compound II.Journal of the American Chemical Society · 2024Article
- Functional Model of Compound II of Cytochrome P450: Spectroscopic Characterization and Reactivity Studies of a FeJACS Au · 2024Article
- Heme-copper and Heme OJournal of inorganic biochemistry · 2023Review
- A sorghum ascorbate peroxidase with four binding sites has activity against ascorbate and phenylpropanoids.Plant physiology · 2023Article
- Interactions of reactive sulfur species with metalloproteins.Redox biology · 2023Review
- Understanding the Key Roles of pH Buffer in Accelerating Lignin Degradation by Lignin Peroxidase.JACS Au · 2023Article
- Common Reactivity and Properties of Heme Peroxidases: A DFT Study of Their Origin.Antioxidants (Basel, Switzerland) · 2023Article
- Activity of Cytosolic Ascorbate Peroxidase (APX) fromInternational journal of molecular sciences · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
Abstract
Catalytic heme enzymes carry out a wide range of oxidations in biology. They have in common a mechanism that requires formation of highly oxidized ferryl intermediates. It is these ferryl intermediates that provide the catalytic engine to drive the biological activity. Unravelling the nature of the ferryl species is of fundamental and widespread importance. The essential question is whether the ferryl is best described as a Fe(IV)=O or a Fe(IV)-OH species, but previous spectroscopic and X-ray crystallographic studies have not been able to unambiguously differentiate between the two species. Here we use a different approach. We report a neutron crystal structure of the ferryl intermediate in Compound II of a heme peroxidase; the structure allows the protonation states of the ferryl heme to be directly observed. This, together with pre-steady state kinetic analyses, electron paramagnetic resonance spectroscopy and single crystal X-ray fluorescence, identifies a Fe(IV)-OH species as the reactive intermediate. The structure establishes a precedent for the formation of Fe(IV)-OH in a peroxidase.
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.