ReviewChemical reviews2022
Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.
Review in Chemical reviews, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 158 citations in OpenAlex.
- Unlocking Distinct Excited States of a Nickel(II) Complex Without Modulating the Primary Coordination Sphere.JACS Au · 2026Article
- Less is more: miniaturized heme enzymes with broad reactivity.Chemical science · 2026Review
- Cyclen Tetra-Amide Ligands as a Privileged Class of Ligands for Studying Second-Sphere Coordination Environments.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Azurins With Tunable Reduction Potentials as Redox Mediators for Extracellular Electron Transfer.Chembiochem : a European journal of chemical biology · 2026Article
- A closely related pair of superoxide dismutase isozymes from Staphylococcus aureus show distinct stabilities and proton-exchange dynamics.The Journal of biological chemistry · 2026Article
- Direct electrochemistry as a mechanistic tool for studying engineered myoglobins: implications on carbene transferase activity.Dalton transactions (Cambridge, England : 2003) · 2026Article
- Probing anion recognition in a cobalt(II) de novo designed metalloprotein.Journal of inorganic biochemistry · 2026Article
- Enantioselective electrophilic α-fluorination catalyzed by an artificial metalloenzyme.Chemical science · 2026Article
- Unraveling the coordination isomerism by ligand hyperfine NMR shifts.Chemical science · 2026Article
- An enzyme's metal preference evolves through redox modulation driven by the cofactor's secondary coordination sphere.Molecular biology and evolution · 2026Article
- Harnessing Photoenzymatic Systems for Intermolecular C-H Fluorination.Angewandte Chemie (International ed. in English) · 2026Article
- Introduction to Carbonic Anhydrase.Sub-cellular biochemistry · 2026Review
- A Minimalist Iron Porphyrin Which Can Catalyze Both Peroxidation and Oxygen Reduction Reaction.JACS Au · 2025Article
- High-resolution X-ray structure of Gln143Asn manganese superoxide dismutase captures multiple hydrogen peroxide-binding sites.Acta crystallographica. Section F, Structural biology communications · 2025Article
- High-Resolution X-ray Structure of Gln143Asn Manganese Superoxide Dismutase Captures Multiple Hydrogen Peroxide Binding Sites.bioRxiv : the preprint server for biology · 2025Article
- Synthesis, Characterization, and Biomolecular Interactions of a novel Copper(II) Complex: DNA and BSA Binding Studies.Journal of fluorescence · 2025Article
- Mechanism of Oxidative C─H Bond Activation by De Novo Designed Artificial Cu Metalloenzymes Using HChemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Synzymes: The Future of Modern Enzyme Engineering.Applied biochemistry and biotechnology · 2025Review
- Hydrogen-Producing Catalysts Based on Ferredoxin Scaffolds.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Regulation of ferryl reactivity by the cytochrome P450 decarboxylase OleT.Journal of inorganic biochemistry · 2025Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Metalloenzymes catalyze a variety of reactions using a limited number of natural amino acids and metallocofactors. Therefore, the environment beyond the primary coordination sphere must play an important role in both conferring and tuning their phenomenal catalytic properties, enabling active sites with otherwise similar primary coordination environments to perform a diverse array of biological functions. However, since the interactions beyond the primary coordination sphere are numerous and weak, it has been difficult to pinpoint structural features responsible for the tuning of activities of native enzymes. Designing artificial metalloenzymes (ArMs) offers an excellent basis to elucidate the roles of these interactions and to further develop practical biological catalysts. In this review, we highlight how the secondary coordination spheres of ArMs influence metal binding and catalysis, with particular focus on the use of native protein scaffolds as templates for the design of ArMs by either rational design aided by computational modeling, directed evolution, or a combination of both approaches. In describing successes in designing heme, nonheme Fe, and Cu metalloenzymes, heteronuclear metalloenzymes containing heme, and those ArMs containing other metal centers (including those with non-native metal ions and metallocofactors), we have summarized insights gained on how careful controls of the interactions in the secondary coordination sphere, including hydrophobic and hydrogen bonding interactions, allow the generation and tuning of these respective systems to approach, rival, and, in a few cases, exceed those of native enzymes. We have also provided an outlook on the remaining challenges in the field and future directions that will allow for a deeper understanding of the secondary coordination sphere a deeper understanding of the secondary coordintion sphere to be gained, and in turn to guide the design of a broader and more efficient variety of ArMs.
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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.