ArticleJournal of the American Chemical Society2019
How [FeFe]-Hydrogenase Facilitates Bidirectional Proton Transfer.
Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 63 citations in OpenAlex.
- Mechanistic Insights into Nitroarene Hydrogenation Dynamics on Pt(111) viaJournal of the American Chemical Society · 2025Article
- Probing the Influence of the Protein Scaffold on H-Cluster Reactivity via Gain-of-Function Studies─Improved HJournal of the American Chemical Society · 2025Article
- Triiron Complexes Featuring Azadiphosphine Related to the Active Site of [FeFe]-Hydrogenases: Their Redox Behavior and Protonation.Molecules (Basel, Switzerland) · 2024Article
- Article
- DNA as a perfect quantum computer based on the quantum physics principles.Scientific reports · 2024Article
- Probing Substrate Transport Effects on Enzymatic Hydrogen Catalysis: An Alternative Proton Transfer Pathway in Putatively Sensory [FeFe] Hydrogenase.ACS catalysis · 2023Article
- A personal account on 25 years of scientific literature on [FeFe]-hydrogenase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023Review
- Phonon-assisted electron-proton transfer in [FeFe] hydrogenases: Topological role of clusters.Biophysical journal · 2023Article
- Binding of exogenous cyanide reveals new active-site states in [FeFe] hydrogenases.Chemical science · 2023Article
- Cyanide Binding to [FeFe]-Hydrogenase Stabilizes the Alternative Configuration of the Proton Transfer Pathway.Angewandte Chemie (International ed. in English) · 2023Article
- Light-Driven [FeFe] Hydrogenase Based HACS sustainable chemistry & engineering · 2022Article
- Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.Chemical reviews · 2022Review
- Hydride state accumulation in native [FeFe]-hydrogenase with the physiological reductant HChemical communications (Cambridge, England) · 2022Article
- Serial crystallography captures dynamic control of sequential electron and proton transfer events in a flavoenzyme.Nature chemistry · 2022Article
- Fast Proton Transport in FeFe Hydrogenase via a Flexible Channel and a Proton Hole Mechanism.The journal of physical chemistry. B · 2022Article
- The Contribution of Proton-Donor pKa on Reactivity Profiles of [FeFe]-hydrogenases.Frontiers in microbiology · 2022Article
- Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture.Chemical science · 2020Article
- The roles of long-range proton-coupled electron transfer in the directionality and efficiency of [FeFe]-hydrogenases.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Metal-ligand cooperativity in the soluble hydrogenase-1 fromChemical science · 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 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hydrogenases are metalloenzymes that catalyze the conversion of protons and molecular hydrogen, H
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.