ArticleProceedings of the National Academy of Sciences of the United States of America2020
Visualizing the protons in a metalloenzyme electron proton transfer pathway.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 31 citations in OpenAlex.
- Mutation of active site glutamate in serine hydroxymethyltransferase allows trapping a reactive intermediate: a combined neutron and X-ray crystallography study.RSC advances · 2026Article
- Solvent Channels and Electric Fields Guide Proton Delivery to the Active Site of Heme Peroxidases.Angewandte Chemie (International ed. in English) · 2025Article
- Unveiling an Ultrareduced State of Heme in Myoglobin.Journal of the American Chemical Society · 2025Article
- Neutron and time-resolved X-ray crystallography reveal the substrate recognition and catalytic mechanism of human Nudix hydrolase MTH1.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Correlating Structure with Spectroscopy in Ascorbate Peroxidase Compound II.Journal of the American Chemical Society · 2024Article
- Comprehensive structural, infrared spectroscopic and kinetic investigations of the roles of the active-site arginine in bidirectional hydrogen activation by the [NiFe]-hydrogenase 'Hyd-2' fromChemical science · 2023Article
- A sorghum ascorbate peroxidase with four binding sites has activity against ascorbate and phenylpropanoids.Plant physiology · 2023Article
- Activity of Cytosolic Ascorbate Peroxidase (APX) fromInternational journal of molecular sciences · 2023Article
- Direct Aerobic Generation of a Ferric Hydroperoxo Intermediate Via a Preorganized Secondary Coordination Sphere.Journal of the American Chemical Society · 2021Article
- Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography.Acta crystallographica. Section D, Structural biology · 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
- Capturing the Catalytic Proton of Dihydrofolate Reductase: Implications for General Acid-Base Catalysis.ACS catalysis · 2021Article
- Production of perdeuterated fucose from glyco-engineered bacteria.Glycobiology · 2021Article
- An Engineered Glutamate in Biosynthetic Models of Heme-Copper Oxidases Drives Complete Product Selectivity by Tuning the Hydrogen-Bonding Network.Biochemistry · 2021Article
- Serial Femtosecond Zero Dose Crystallography Captures a Water-Free Distal Heme Site in a Dye-Decolorising Peroxidase to Reveal a Catalytic Role for an Arginine in FeAngewandte Chemie (International ed. in English) · 2020Article
- Structure-activity relationship and mechanism of four monostilbenes with respect to ferroptosis inhibition.RSC advances · 2020Article
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 at 5 institutions in 3 countries.
Funding
Abstract
In redox metalloenzymes, the process of electron transfer often involves the concerted movement of a proton. These processes are referred to as proton-coupled electron transfer, and they underpin a wide variety of biological processes, including respiration, energy conversion, photosynthesis, and metalloenzyme catalysis. The mechanisms of proton delivery are incompletely understood, in part due to an absence of information on exact proton locations and hydrogen bonding structures in a bona fide metalloenzyme proton pathway. Here, we present a 2.1-Å neutron crystal structure of the complex formed between a redox metalloenzyme (ascorbate peroxidase) and its reducing substrate (ascorbate). In the neutron structure of the complex, the protonation states of the electron/proton donor (ascorbate) and all of the residues involved in the electron/proton transfer pathway are directly observed. This information sheds light on possible proton movements during heme-catalyzed oxygen activation, as well as on ascorbate oxidation.
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.