ArticleChemical science2020
Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture.
Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- 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
- 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
- H-cluster Intermediates and Catalytic Properties ofBiochemistry · 2025Article
- A [FeFe] Hydrogenase-Rubrerythrin Chimeric Enzyme Functions to Couple HJournal 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
- Article
- Outer-sphere effects on the OChemical science · 2024Review
- Kinetic Modeling of the Reversible or Irreversible Electrochemical Responses of FeFe-Hydrogenases.Journal of the American Chemical Society · 2024Article
- Developing high-affinity, oxygen-insensitive [NiFe]-hydrogenases as biocatalysts for energy conversion.Biochemical Society transactions · 2023Review
- 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
- Redox tuning of the H-cluster by second coordination sphere amino acids in the sensory [FeFe] hydrogenase fromChemical science · 2023Article
- Investigating the role of the strong field ligands in [FeFe] hydrogenase: spectroscopic and functional characterization of a semi-synthetic mono-cyanide active site.Chemical science · 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
- Fantastic [FeFe]-Hydrogenases and Where to Find Them.Frontiers in microbiology · 2022Review
- Improving sustainable hydrogen production from green waste: [FeFe]-hydrogenases quantitative gene expression RT-qPCR analysis in presence of autochthonous consortia.Biotechnology for biofuels · 2021Article
- Reversible catalysis.Nature reviews. Chemistry · 2021Review
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
[FeFe]-hydrogenases are known for their high rates of hydrogen turnover, and are intensively studied in the context of biotechnological applications. Evolution has generated a plethora of different subclasses with widely different characteristics. The M2e subclass is phylogenetically distinct from previously characterized members of this enzyme family and its biological role is unknown. It features significant differences in domain- and active site architecture, and is most closely related to the putative sensory [FeFe]-hydrogenases. Here we report the first comprehensive biochemical and spectroscopical characterization of an M2e enzyme, derived from
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