ReviewNature reviews. Microbiology2013
Structure, function and biosynthesis of O₂-tolerant hydrogenases.
Review in Nature reviews. Microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 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
57 citing papers in PubMed.
- Application of Molecular Hydrogen as an Antioxidant in Responses to Ventilatory and Ergogenic Adjustments during Incremental Exercise in Humans.Nutrients · 2021Trial
- Genomically integrated orthogonal translation system in Escherichia coli enables production of functional modified [NiFe]-hydrogenases.Microbial cell factories · 2026Article
- NRVS Spectroscopy Resolves Distinct Bridging Hydride Intermediates in [NiFe]-Hydrogenase.Journal of the American Chemical Society · 2025Article
- Fortification of FeS Clusters Reshapes Anaerobic CO Dehydrogenase into an Air-Viable Enzyme Through Multilayered Sealing of OAngewandte Chemie (International ed. in English) · 2025Article
- Biosynthesis and assembly of hydrogenase [NiFe]-cofactor: recent advances and perspectives.Metallomics : integrated biometal science · 2025Review
- Fully Oxidized State of the Oxygen-Tolerant [NiFe] Hydrogenase fromInorganic chemistry · 2025Article
- Reactivation and long-term stabilization of the [NiFe] Hox hydrogenase of Synechocystis sp. PCC6803 by glutathione after oxygen exposure.The Journal of biological chemistry · 2025Article
- The energy metabolism ofApplied and environmental microbiology · 2024Article
- Strain and model development for auto- and heterotrophic 2,3-butanediol production using Cupriavidus necator H16.Biotechnology for biofuels and bioproducts · 2024Article
- Characterization of the Bottlenecks and Pathways for Inhibitor Dissociation from [NiFe] Hydrogenase.Journal of chemical information and modeling · 2024Article
- Unveiling the Low-Lying Spin States of [FeMolecules (Basel, Switzerland) · 2024Article
- Developing high-affinity, oxygen-insensitive [NiFe]-hydrogenases as biocatalysts for energy conversion.Biochemical Society transactions · 2023Review
- Stepwise conversion of the CysChemical science · 2023Article
- Stepwise assembly of the active site of [NiFe]-hydrogenase.Nature chemical biology · 2023Article
- Implementation of a high cell density fed-batch for heterologous production of active [NiFe]-hydrogenase in Escherichia coli bioreactor cultivations.Microbial cell factories · 2022Article
- Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.Chemical reviews · 2022Review
- Molecular hydrogen is a promising therapeutic agent for pulmonary disease.Journal of Zhejiang University. Science. B · 2022Article
- High-Yield Production of Catalytically Active Regulatory [NiFe]-Hydrogenase FromFrontiers in microbiology · 2022Article
- Optimization of Culture Conditions for Oxygen-Tolerant Regulatory [NiFe]-Hydrogenase Production fromMicroorganisms · 2021Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular hydrogen (H(2)) is used as an energy source or a way to deposit excess reducing power by a wide range of microorganisms. Both H(2) oxidation and production are catalysed by hydrogenases. As these metalloenzymes are usually exquisitely O(2) sensitive, H(2) metabolism under aerobic conditions, which is known as O(2)-tolerant H(2) cycling, involves hydrogenases that have undergone structural and catalytic adaptations and requires a dedicated biosynthetic machinery. Here, we discuss recent high-resolution crystal structure analyses of a particular subtype of [NiFe]-hydrogenase that is predominantly found in aerobic or facultative aerobic H(2)-oxidizing bacteria. These data have provided insights into the underlying molecular strategies that allow sustained biological conversion of H(2) in the presence of O(2).
Indexed as
Identifiers
23321533What 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.