Rational design of metalloenzymes: From single to multiple active sites
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Summary
This review summarizes the recent achievements in rational design of metalloenzymes from single to multiple active sites in natural or de novo protein scaffolds, with a diverse range of functionalities, even beyond those of natural metall Koenzymes.
- Type
- article
- Published
- 2017-04-01
- Cited by
- 126
- References
- 230
- Access
- Open access
- OpenAlex
- https://openalex.org/W2569641753
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:99394811
Keywords
Chemistry, Rational design, Protein design, Active site, Protein engineering
References
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Cited by
- Molecular magnetism, quo vadis? A historical perspective from a coordination chemist viewpoint☆
- Understanding the choice of copper by heme-copper oxidase using biosynthetic models in myoglobin
- Peroxidase Activity of a c‐Type Cytochrome b 5 in the Non‐Native State is Comparable to that of Native Peroxidases
- Control of Heme Coordination and Catalytic Activity by Conformational Changes in Peptide-Amphiphile Assemblies.
- Synthetic Analogues of Nitrogenase Metallocofactors: Challenges and Developments.
- Rational design of artificial dye-decolorizing peroxidases using myoglobin by engineering Tyr/Trp in the heme center.
- Mimicking a Natural Enzyme System: Cytochrome c Oxidase-Like Activity of Cu2O Nanoparticles by Receiving Electrons from Cytochrome c.
- Small iron-carbonyl clusters bearing imidazolium-2-trithioperoxycarboxylate ligands.
- Review for chiral-at-metal complexes and metal-organic framework enantiomorphs.
- Streptavidin as a Scaffold for Light-Induced Long-Lived Charge Separation.
- Photo-induced DNA cleavage by zinc-substituted myoglobin with a redesigned active center
- A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-Dependent Oxidation.
- Understanding and Designing Head-to-Tail Cyclic Peptides
- Nitrite Reduction in Aqueous Solution Mediated by Amavadin Homologues: N2 O Formation and Water Oxidation.
- Stabilization of synthetic heme-superoxo complexes by hydrogen bonding: a still on-going quest
- Functionalization of protein crystals with metal ions, complexes and nanoparticles.
- Design of artificial metalloproteins/metalloenzymes by tuning noncovalent interactions
- Global Structural Flexibility of Metalloproteins Regulates Reactivity of Transition Metal Ion in the Protein Core: An Experimental Study Using Thiol-subtilisin as a Model Protein.
- From protein engineering to artificial enzymes – biological and biomimetic approaches towards sustainable hydrogen production
- Proteins as Macromolecular Ligands for Metal‐Catalysed Asymmetric Transfer Hydrogenation of Ketones in Aqueous Medium
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