ArticleNature2013
Biomimetic assembly and activation of [FeFe]-hydrogenases.
Article in Nature, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 193 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
193 citing papers in PubMed, 678 citations in OpenAlex.
- A Gas Chromatography-Based Workflow Leads to the Detection of Hydrogenase Activity in Native Bacteria.Chembiochem : a European journal of chemical biology · 2026Article
- Synthesis of diiron subcluster [FeNature protocols · 2026Review
- A Non-Covalent [4Fe-4S]/[2Fe] Interface in HydF Guides [FeFe]-Hydrogenase Maturation.Angewandte Chemie (International ed. in English) · 2026Article
- Biosynthesis of the Selenium-Substituted [FeFe]-Hydrogenases.Journal of the American Chemical Society · 2026Article
- Two-Dimensional Infrared Spectroscopy Reveals the Presence of a Bridging CO Ligand in Two Catalytic Intermediates of [FeFe] Hydrogenase.Angewandte Chemie (International ed. in English) · 2026Article
- Subunit fusion unlocks rapidChemical science · 2026Article
- Probing the Role of Accessory FeS Clusters in Putative Sensory Group D [FeFe] Hydrogenase: Influence of the C-Terminal [4Fe-4S] Cluster on the Reactivity ofBiochemistry · 2026Article
- [FeFe] hydrogenases with modified azadithiolate bridgeheads serve as unidirectional hydrogen oxidation catalysts.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026Article
- Probing Hydrogen Activation in a Dimetal Dihydride Complex by Symmetric Exchange with Parahydrogen.Journal of the American Chemical Society · 2026Article
- The [4Fe-4S] Cluster of HydF Is Essential for [FeFe]-Hydrogenase Maturation.Journal of the American Chemical Society · 2025Article
- Decoding the Elusive Redox Properties of [FeS] Clusters in [FeFe]-Hydrogenase on a Nanostructured Electrode.Journal of the American Chemical Society · 2025Article
- Reconsidering the Enzyme Kinetics of [FeFe]-Hydrogenases: Improved Turnover Rates and New Insights into pH and Potential Dependence with Eu(II)-Based Solution Assays.Analytical chemistry · 2025Article
- Engineering the Electron Relay in [FeFe]-Hydrogenase Enhances Electrocatalytic HACS catalysis · 2025Article
- A widespread hydrogenase supports fermentative growth of gut bacteria in healthy people.Nature microbiology · 2025Article
- Turning the FeFe hydrogenase fromProceedings of the National Academy of Sciences of the United States of America · 2025Article
- In vitro maturation of fully active [FeFe]-hydrogenase in a defined system including the iron carrier NfuA.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- NRVS of FeS cluster proteins & models - A bestiary of nifty normal modes.Journal of inorganic biochemistry · 2025Review
- Hydrogen-Producing Catalysts Based on Ferredoxin Scaffolds.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Mechanistic Promiscuity in Cobalt-Mediated COAngewandte Chemie (International ed. in English) · 2025Article
- Computational Modeling and Experimental Approaches for Understanding the Mechanisms of [FeFe]-Hydrogenase.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
133 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
13 authors at 8 institutions in 3 countries.
Funding
Abstract
Hydrogenases are the most active molecular catalysts for hydrogen production and uptake, and could therefore facilitate the development of new types of fuel cell. In [FeFe]-hydrogenases, catalysis takes place at a unique di-iron centre (the [2Fe] subsite), which contains a bridging dithiolate ligand, three CO ligands and two CN(-) ligands. Through a complex multienzymatic biosynthetic process, this [2Fe] subsite is first assembled on a maturation enzyme, HydF, and then delivered to the apo-hydrogenase for activation. Synthetic chemistry has been used to prepare remarkably similar mimics of that subsite, but it has failed to reproduce the natural enzymatic activities thus far. Here we show that three synthetic mimics (containing different bridging dithiolate ligands) can be loaded onto bacterial Thermotoga maritima HydF and then transferred to apo-HydA1, one of the hydrogenases of Chlamydomonas reinhardtii algae. Full activation of HydA1 was achieved only when using the HydF hybrid protein containing the mimic with an azadithiolate bridge, confirming the presence of this ligand in the active site of native [FeFe]-hydrogenases. This is an example of controlled metalloenzyme activation using the combination of a specific protein scaffold and active-site synthetic analogues. This simple methodology provides both new mechanistic and structural insight into hydrogenase maturation and a unique tool for producing recombinant wild-type and variant [FeFe]-hydrogenases, with no requirement for the complete maturation machinery.
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.