ArticleNature chemistry2015
Reconstitution of [Fe]-hydrogenase using model complexes.
Article in Nature chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 104 citations in OpenAlex.
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- Artificial Small Molecules as Cofactors and Biomacromolecular Building Blocks in Synthetic Biology: Design, Synthesis, Applications, and Challenges.Molecules (Basel, Switzerland) · 2023Review
- Stepwise assembly of the active site of [NiFe]-hydrogenase.Nature chemical biology · 2023Article
- Hydrogenase and Nitrogenase: Key Catalysts in Biohydrogen Production.Molecules (Basel, Switzerland) · 2023Review
- Scaffold-based [Fe]-hydrogenase model: HChemical science · 2021Article
- Diversifying Metal-Ligand Cooperative Catalysis in Semi-Synthetic [Mn]-Hydrogenases.Angewandte Chemie (International ed. in English) · 2021Article
- Optimization of Culture Conditions for Oxygen-Tolerant Regulatory [NiFe]-Hydrogenase Production fromMicroorganisms · 2021Article
- Artificial Metalloenzymes: From Selective Chemical Transformations to Biochemical Applications.Molecules (Basel, Switzerland) · 2020Review
- Methanogenesis involves direct hydride transfer from HNature reviews. Chemistry · 2020Review
- A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor.Nature chemistry · 2019Article
- A low-valent dinuclear ruthenium diazadiene complex catalyzes the oxidation of dihydrogen and reversible hydrogenation of quinones.Chemical science · 2019Article
- Tracing the 'ninth sulfur' of the nitrogenase cofactor via a semi-synthetic approach.Nature chemistry · 2018Article
- From protein engineering to artificial enzymes - biological and biomimetic approaches towards sustainable hydrogen production.Sustainable energy & fuels · 2018Review
- Article
- Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides.Chemical reviews · 2016Review
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
[Fe]-Hydrogenase catalyses the reversible hydrogenation of a methenyltetrahydromethanopterin substrate, which is an intermediate step during the methanogenesis from CO2 and H2. The active site contains an iron-guanylylpyridinol cofactor, in which Fe(2+) is coordinated by two CO ligands, as well as an acyl carbon atom and a pyridinyl nitrogen atom from a 3,4,5,6-substituted 2-pyridinol ligand. However, the mechanism of H2 activation by [Fe]-hydrogenase is unclear. Here we report the reconstitution of [Fe]-hydrogenase from an apoenzyme using two FeGP cofactor mimics to create semisynthetic enzymes. The small-molecule mimics reproduce the ligand environment of the active site, but are inactive towards H2 binding and activation on their own. We show that reconstituting the enzyme using a mimic that contains a 2-hydroxypyridine group restores activity, whereas an analogous enzyme with a 2-methoxypyridine complex was essentially inactive. These findings, together with density functional theory computations, support a mechanism in which the 2-hydroxy group is deprotonated before it serves as an internal base for heterolytic H2 cleavage.
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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.