ArticleProceedings of the National Academy of Sciences of the United States of America2016
Design of a single protein that spans the entire 2-V range of physiological redox potentials.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Azurins With Tunable Reduction Potentials as Redox Mediators for Extracellular Electron Transfer.Chembiochem : a European journal of chemical biology · 2026Article
- An enzyme's metal preference evolves through redox modulation driven by the cofactor's secondary coordination sphere.Molecular biology and evolution · 2026Article
- Article
- Beyond Blue: Systematic Modulation of Electronic Structure and Redox Properties of Type 1 Copper in Azurin.Journal of the American Chemical Society · 2025Article
- Azurin: A Model to Study a Metal Coordination Sphere or Electron Transfer in Metalloproteins.International journal of molecular sciences · 2025Review
- Development of artificial photosystems based on designed proteins for mechanistic insights into photosynthesis.Protein science : a publication of the Protein Society · 2024Review
- Beyond the coupled distortion model: structural analysis of the single domain cupredoxin AcoP, a green mononuclear copper centre with original features.Dalton transactions (Cambridge, England : 2003) · 2024Article
- Electrochemical and structural characterization of recombinant respiratory proteins of the acidophilic iron oxidizerFrontiers in microbiology · 2024Article
- Increasing Reduction Potentials of Type 1 Copper Center and Catalytic Efficiency of Small Laccase from Streptomyces coelicolor through Secondary Coordination Sphere Mutations.Angewandte Chemie (International ed. in English) · 2023Article
- Mechanisms and Opportunities for Rational In Silico Design of Enzymes to Degrade Per- and Polyfluoroalkyl Substances (PFAS).Journal of chemical information and modeling · 2023Review
- A designed Copper Histidine-brace enzyme for oxidative depolymerization of polysaccharides as a model of lytic polysaccharide monooxygenase.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Mechanism of Inhibition of Pyruvate Formate Lyase by Methacrylate.Journal of the American Chemical Society · 2023Article
- Primary and Secondary Coordination Sphere Effects on the Structure and Function ofJournal of the American Chemical Society · 2023Article
- Charge Regulation in a Rieske Proton Pump Pinpoints Zero, One, and Two Proton-Coupled Electron Transfer.Journal of the American Chemical Society · 2023Article
- AMOEBA Force Field Predicts Accurate Hydrogen Bond Counts of Nitriles in SNase by Revealing Water-Protein Interaction in Vibrational Absorption Frequencies.The journal of physical chemistry. B · 2023Article
- Tuning the Type 1 Reduction Potential of Multicopper Oxidases: Uncoupling the Effects of Electrostatics and H-Bonding to Histidine Ligands.Journal of the American Chemical Society · 2023Article
- Classifying metal-binding sites with neural networks.Protein science : a publication of the Protein Society · 2023Article
- Engineering a Conformationally Switchable Artificial Metalloprotein.Journal of the American Chemical Society · 2022Article
- AMOEBA Force Field Trajectories Improve Predictions of Accurate pThe journal of physical chemistry. B · 2022Article
- Fine-tuning of FeS proteins monitored via pulsed EPR redox potentiometry at Q-band.Biophysical reports · 2021Article
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Abstract
The reduction potential (E°') is a critical parameter in determining the efficiency of most biological and chemical reactions. Biology employs three classes of metalloproteins to cover the majority of the 2-V range of physiological E°'s. An ultimate test of our understanding of E°' is to find out the minimal number of proteins and their variants that can cover this entire range and the structural features responsible for the extreme E°'. We report herein the design of the protein azurin to cover a range from +970 mV to -954 mV vs. standard hydrogen electrode (SHE) by mutating only five residues and using two metal ions. Spectroscopic methods have revealed geometric parameters important for the high E°'. The knowledge gained and the resulting water-soluble redox agents with predictable E°'s, in the same scaffold with the same surface properties, will find wide applications in chemical, biochemical, biophysical, and biotechnological fields.
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