ArticleAngewandte Chemie (International ed. in English)2015
Combining a Nitrogenase Scaffold and a Synthetic Compound into an Artificial Enzyme.
Article in Angewandte Chemie (International ed. in English), 2015. 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
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
10 citing papers in PubMed.
- Catalytic Reduction of Cyanide to Ammonia and Methane at a Mononuclear Fe Site.Journal of the American Chemical Society · 2024Article
- Enzymatic Fischer-Tropsch-Type Reactions.Chemical reviews · 2023Review
- Incorporation of an Asymmetric Mo-Fe-S Cluster as an Artificial Cofactor into Nitrogenase.Chembiochem : a European journal of chemical biology · 2022Article
- Reconstruction of Nitrogenase Predecessors Suggests Origin from Maturase-Like Proteins.Genome biology and evolution · 2022Article
- Repurposing metalloproteins as mimics of natural metalloenzymes for small-molecule activation.Journal of inorganic biochemistry · 2021Review
- Rational Design of Artificial Metalloproteins and Metalloenzymes with Metal Clusters.Molecules (Basel, Switzerland) · 2019Review
- 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
- Proton-Coupled Reduction of an Iron Cyanide Complex to Methane and Ammonia.Angewandte Chemie (International ed. in English) · 2016Article
- Insight into the Iron-Molybdenum Cofactor of Nitrogenase from Synthetic Iron Complexes with Sulfur, Carbon, and Hydride Ligands.Journal of the American Chemical Society · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Nitrogenase catalyzes substrate reduction at its cofactor center ([(Cit)MoFe7S9C](n-); designated M-cluster). Here, we report the formation of an artificial, nitrogenase-mimicking enzyme upon insertion of a synthetic model complex ([Fe6S9(SEt)2](4-); designated Fe6(RHH)) into the catalytic component of nitrogenase (designated NifDK(apo)). Two Fe6(RHH) clusters were inserted into NifDK(apo), rendering the conformation of the resultant protein (designated NifDK(Fe)) similar to the one upon insertion of native M-clusters. NifDK(Fe) can work together with the reductase component of nitrogenase to reduce C2H2 in an ATP-dependent reaction. It can also act as an enzyme on its own in the presence of Eu(II)DTPA, displaying a strong activity in C2H2 reduction while demonstrating an ability to reduce CN(-) to C1-C3 hydrocarbons in an ATP-independent manner. The successful outcome of this work provides the proof of concept and underlying principles for continued search of novel enzymatic activities based on this approach.
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.