ArticleScientific reports2016
Construction of a subunit-fusion nitrile hydratase and discovery of an innovative metal ion transfer pattern.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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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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.
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Who cites it
6 citing papers in PubMed, 21 citations in OpenAlex.
- A Versatile Protein Scaffold Engineered for the Hierarchical Assembly of Robust and Highly Active Enzymes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Oligomeric interactions maintain active-site structure in a noncooperative enzyme family.The EMBO journal · 2022Article
- Computational Design of Nitrile Hydratase fromMolecules (Basel, Switzerland) · 2020Article
- Efficient Overproduction of Active Nitrile Hydratase by Coupling Expression Induction and Enzyme MaturationFrontiers in bioengineering and biotechnology · 2020Article
- Recent Advances and Promises in Nitrile Hydratase: From Mechanism to Industrial Applications.Frontiers in bioengineering and biotechnology · 2020Review
- Advances in cloning, structural and bioremediation aspects of nitrile hydratases.Molecular biology reports · 2019Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Metallochaperones are metal-binding proteins designed to deliver the appropriate metal to a target protein. The metal is usually transferred between different proteins. In this study, we discovered that metal was transferred between the same subunit of a mutant nitrile hydratase (NHase). Various "activator proteins" mediate the trafficking of metal ions into NHases. We constructed fusion NHases by fusing the β- and α-subunits and/or the "activator proteins" of the NHase from Pseudomonas putida. The fusion NHases exhibited higher thermostability and tolerance to high concentrations of the product amide. The mechanism of the cobalt incorporation changed from a self-subunit swapping pattern to an apoprotein-specific molecular chaperone pattern in vivo and a metallochaperone pattern in vitro. Notably, the cobalt transfer occurred between the same α-subunit in the metallochaperone pattern. These results not only demonstrated the superiority of fusion-type NHases, but also revealed an innovative metal ion transfer pattern in metalloprotein biosynthesis.
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Registered trials
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