ArticleChemical science2017
Infrared spectroscopy of the nitrogenase MoFe protein under electrochemical control: potential-triggered CO binding.
Article in Chemical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed, 48 citations in OpenAlex.
- Structural Characterization of Four Redox States of the P-cluster in Molybdenum Nitrogenase via Electrochemical Control of Crystals.Journal of the American Chemical Society · 2026Article
- Investigating the Molybdenum Nitrogenase Mechanistic Cycle Using Spectroelectrochemistry.Journal of the American Chemical Society · 2025Article
- Electrochemical experiments define potentials associated with binding of substrates and inhibitors to nitrogenase MoFe protein.Faraday discussions · 2023Article
- Enzymatic and Microbial Electrochemistry: Approaches and Methods.ACS measurement science au · 2022Review
- Carbon monoxide binding to α-R277H Mo-nitrogenase - Evidence for multiple pH-dependent species from IR-monitored photolysis.Journal of inorganic biochemistry · 2022Article
- The Conversion of Carbon Monoxide and Carbon Dioxide by Nitrogenases.Chembiochem : a European journal of chemical biology · 2022Review
- The crystalline state as a dynamic system: IR microspectroscopy under electrochemical control for a [NiFe] hydrogenase.Chemical science · 2021Article
- Electrochemical control of [FeFe]-hydrogenase single crystals reveals complex redox populations at the catalytic site.Dalton transactions (Cambridge, England : 2003) · 2021Article
- Reduction of Substrates by Nitrogenases.Chemical reviews · 2020Review
- The Spectroscopy of Nitrogenases.Chemical reviews · 2020Review
- Spectroscopic Description of the EInorganic chemistry · 2019Article
- Beyond fossil fuel-driven nitrogen transformations.Science (New York, N.Y.) · 2018Review
- A Thermodynamic Model for Redox-Dependent Binding of Carbon Monoxide at Site-Differentiated, High Spin Iron Clusters.Journal of the American Chemical Society · 2018Article
- Nitrogen Reduction to Ammonia on a Biomimetic Mononuclear Iron Centre: Insights into the Nitrogenase Enzyme.Chemistry (Weinheim an der Bergstrasse, Germany) · 2018Article
- Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase.Journal of visualized experiments : JoVE · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We demonstrate electrochemical control of the nitrogenase MoFe protein, in the absence of Fe protein or ATP, using europium(iii/ii) polyaminocarboxylate complexes as electron transfer mediators. This allows the potential dependence of proton reduction and inhibitor (CO) binding to the active site FeMo-cofactor to be established. Reduction of protons to H
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.