ArticleProceedings of the National Academy of Sciences of the United States of America2014
How oxygen reacts with oxygen-tolerant respiratory [NiFe]-hydrogenases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 93 citations in OpenAlex.
- Rational engineering of facultative anaerobiosis enables commensal survival in the oxygenated gut.bioRxiv : the preprint server for biology · 2026Article
- Lessons, connections, hypotheses and predictions from protein film electrochemistry.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026Review
- Fully Oxidized State of the Oxygen-Tolerant [NiFe] Hydrogenase fromInorganic chemistry · 2025Article
- Application of lactose based autoinduction for heterologous production of an active [NiFe] hydrogenase in E. coli.Biotechnology letters · 2025Article
- Developing high-affinity, oxygen-insensitive [NiFe]-hydrogenases as biocatalysts for energy conversion.Biochemical Society transactions · 2023Review
- Stepwise conversion of the CysChemical science · 2023Article
- Safe, One-Pot, Homogeneous Direct Synthesis of HJournal of the American Chemical Society · 2023Article
- Article
- Real flue gas COFrontiers in bioengineering and biotechnology · 2023Article
- Hydrogen-fueled COFrontiers in bioengineering and biotechnology · 2022Article
- E. coli Nickel-Iron Hydrogenase 1 Catalyses Non-native Reduction of Flavins: Demonstration for Alkene Hydrogenation by Old Yellow Enzyme Ene-reductases*.Angewandte Chemie (International ed. in English) · 2021Article
- Article
- Selective cysteine-to-selenocysteine changes in a [NiFe]-hydrogenase confirm a special position for catalysis and oxygen tolerance.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- From protein engineering to artificial enzymes - biological and biomimetic approaches towards sustainable hydrogen production.Sustainable energy & fuels · 2018Review
- Tracking the route of molecular oxygen in OProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Mechanism of ONature chemistry · 2017Article
- Characterization of [FeFe] Hydrogenase O2 Sensitivity Using a New, Physiological Approach.The Journal of biological chemistry · 2016Article
- Anaerobic Formate and Hydrogen Metabolism.EcoSal Plus · 2016Review
- Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides.Chemical reviews · 2016Review
- How the oxygen tolerance of a [NiFe]-hydrogenase depends on quaternary structure.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
An oxygen-tolerant respiratory [NiFe]-hydrogenase is proven to be a four-electron hydrogen/oxygen oxidoreductase, catalyzing the reaction 2 H2 + O2 = 2 H2O, equivalent to hydrogen combustion, over a sustained period without inactivating. At least 86% of the H2O produced by Escherichia coli hydrogenase-1 exposed to a mixture of 90% H2 and 10% O2 is accounted for by a direct four-electron pathway, whereas up to 14% arises from slower side reactions proceeding via superoxide and hydrogen peroxide. The direct pathway is assigned to O2 reduction at the [NiFe] active site, whereas the side reactions are an unavoidable consequence of the presence of low-potential relay centers that release electrons derived from H2 oxidation. The oxidase activity is too slow to be useful in removing O2 from the bacterial periplasm; instead, the four-electron reduction of molecular oxygen to harmless water ensures that the active site survives to catalyze sustained hydrogen oxidation.
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.