ArticleChemical science2023
Redox tuning of the H-cluster by second coordination sphere amino acids in the sensory [FeFe] hydrogenase from
Article in Chemical science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Genomically integrated orthogonal translation system in Escherichia coli enables production of functional modified [NiFe]-hydrogenases.Microbial cell factories · 2026Article
- Article
- 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
- Quantum Life Science: A Paradigm for Life Science Research.ACS nano · 2026Review
- Decoding the Elusive Redox Properties of [FeS] Clusters in [FeFe]-Hydrogenase on a Nanostructured Electrode.Journal 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
- Outer-sphere effects on the OChemical science · 2024Review
- Understanding the [NiFe] Hydrogenase Active Site Environment through Ultrafast Infrared and 2D-IR Spectroscopy of the Subsite Analogue K[CpFe(CO)(CN)The journal of physical chemistry. B · 2024Article
- Kinetic Modeling of the Reversible or Irreversible Electrochemical Responses of FeFe-Hydrogenases.Journal of the American Chemical Society · 2024Article
- Probing Substrate Transport Effects on Enzymatic Hydrogen Catalysis: An Alternative Proton Transfer Pathway in Putatively Sensory [FeFe] Hydrogenase.ACS catalysis · 2023Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
[FeFe] hydrogenases are exceptionally active catalysts for the interconversion of molecular hydrogen with protons and electrons. Their active site, the H-cluster, is composed of a [4Fe-4S] cluster covalently linked to a unique [2Fe] subcluster. These enzymes have been extensively studied to understand how the protein environment tunes the properties of the Fe ions for efficient catalysis. The sensory [FeFe] hydrogenase (HydS) from
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.