ArticleThe Journal of biological chemistry2011
Nature of the ferryl heme in compounds I and II.
Article in The Journal of biological chemistry, 2011. 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 51 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
51 citing papers in PubMed, 111 citations in OpenAlex.
- 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
- Bacterial cytochrome P450 for oxidative halogenated biaryl coupling.ACS catalysis · 2026Article
- Can ferric-oxyl excited states explain elongated iron-oxygen bonds in heme peroxidase catalytic intermediates?Nature communications · 2026Article
- Designing an ecofriendly catalyst for a sustainable use of water resources.National science review · 2026Article
- Solvent Channels and Electric Fields Guide Proton Delivery to the Active Site of Heme Peroxidases.Angewandte Chemie (International ed. in English) · 2025Article
- Role of Propionate Side Chain in Heme-Containing Metalloenzymes.ACS organic & inorganic Au · 2025Review
- Stabilization of the Ferryl═Oxoheme Form ofJournal of the American Chemical Society · 2025Article
- Exploring the Ascorbate Requirement of the 2-Oxoglutarate-Dependent Dioxygenases.Journal of medicinal chemistry · 2025Review
- Competing Reaction Pathways in Gas-Phase Oxidation of CThe journal of physical chemistry. A · 2024Article
- Correlating Structure with Spectroscopy in Ascorbate Peroxidase Compound II.Journal of the American Chemical Society · 2024Article
- Structural Characterization ofInternational journal of molecular sciences · 2023Article
- Common Reactivity and Properties of Heme Peroxidases: A DFT Study of Their Origin.Antioxidants (Basel, Switzerland) · 2023Article
- Exploring the Factors which Result in Cytochrome P450 Catalyzed Desaturation Versus Hydroxylation.Chemistry, an Asian journal · 2022Article
- Article
- Mechanistic insights into the chemistry of compound I formation in heme peroxidases: quantum chemical investigations of cytochromeRSC advances · 2022Article
- Cryo-EM structures of intermediates suggest an alternative catalytic reaction cycle for cytochrome c oxidase.Nature communications · 2021Article
- Functional and protective hole hopping in metalloenzymes.Chemical science · 2021Review
- Aspartate or arginine? Validated redox state X-ray structures elucidate mechanistic subtleties of FeJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Review
- XFEL Crystal Structures of Peroxidase Compound II.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021Article
- XFEL Crystal Structures of Peroxidase Compound II.Angewandte Chemie (International ed. in English) · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Heme enzymes are ubiquitous in biology and catalyze a vast array of biological redox processes. The formation of high valent ferryl intermediates of the heme iron (known as Compounds I and Compound II) is implicated for a number of catalytic heme enzymes, but these species are formed only transiently and thus have proved somewhat elusive. In consequence, there has been conflicting evidence as to the nature of these ferryl intermediates in a number of different heme enzymes, in particular the precise nature of the bond between the heme iron and the bound oxygen atom. In this work, we present high resolution crystal structures of both Compound I and Compound II intermediates in two different heme peroxidase enzymes, cytochrome c peroxidase and ascorbate peroxidase, allowing direct and accurate comparison of the bonding interactions in the different intermediates. A consistent picture emerges across all structures, showing lengthening of the ferryl oxygen bond (and presumed protonation) on reduction of Compound I to Compound II. These data clarify long standing inconsistencies on the nature of the ferryl heme species in these intermediates.
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.