ArticleJournal of the American Chemical Society2016
Modular Artificial Cupredoxins.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Enantioselective electrophilic α-fluorination catalyzed by an artificial metalloenzyme.Chemical science · 2026Article
- Copper-oxygen adducts: new trends in characterization and properties towards C-H activation.Chemical science · 2024Review
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- Review
- Artificial Metalloproteins with Dinuclear Iron-Hydroxido Centers.Journal of the American Chemical Society · 2021Article
- Aromatic foldamers as scaffolds for metal second coordination sphere design.Chemical science · 2020Article
- Traversing the Red-Green-Blue Color Spectrum in Rationally Designed Cupredoxins.Journal of the American Chemical Society · 2020Article
- Artificial Iron Proteins: Modeling the Active Sites in Non-Heme Dioxygenases.Inorganic chemistry · 2020Article
- Rational Design of a Histidine-Methionine Site Modeling the M-Center of Copper Monooxygenases in a Small Metallochaperone Scaffold.Biochemistry · 2019Article
- Redesign of a Copper Storage Protein into an Artificial Hydrogenase.ACS catalysis · 2019Article
- Clarifying the Copper Coordination Environment in a de Novo Designed Red Copper Protein.Inorganic chemistry · 2018Article
- Coordination chemistry within a protein host: regulation of the secondary coordination sphere.Chemical communications (Cambridge, England) · 2018Article
- Artificial Metalloproteins Containing CoJournal of the American Chemical Society · 2018Article
- Peroxide Activation Regulated by Hydrogen Bonds within Artificial Cu Proteins.Journal of the American Chemical Society · 2017Article
- Computational approaches forBioscience reports · 2017Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Cupredoxins are electron-transfer proteins that have active sites containing a mononuclear Cu center with an unusual trigonal monopyramidal structure (Type 1 Cu). A single Cu-Scys bond is present within the trigonal plane that is responsible for its unique physical properties. We demonstrate that a cysteine-containing variant of streptavidin (Sav) can serve as a protein host to model the structure and properties of Type 1 Cu sites. A series of artificial Cu proteins are described that rely on Sav and a series of biotinylated synthetic Cu complexes. Optical and EPR measurements highlight the presence of a Cu-Scys bond, and XRD analysis provides structural evidence. We further provide evidence that changes in the linker between the biotin and Cu complex within the synthetic constructs allows for small changes in the placement of Cu centers within Sav that have dramatic effects on the structural and physical properties of the resulting artificial metalloproteins. These findings highlight the utility of the biotin-Sav technology as an approach for simulating active sites of metalloproteins.
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Registered trials
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