ArticleProceedings of the National Academy of Sciences of the United States of America2013
Designed azurins show lower reorganization free energies for intraprotein electron transfer.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. 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.
- Controlling outer-sphere solvent reorganization energy to turn on or off the function of artificial metalloenzymes.Nature communications · 2025Article
- Pyruvate dehydrogenase operates as an intramolecular nitroxyl generator during macrophage metabolic reprogramming.Nature communications · 2023Article
- Why charging Li-air batteries with current low-voltage mediators is slow and singlet oxygen does not explain degradation.Nature chemistry · 2023Article
- Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.Chemical reviews · 2022Review
- CuChemical science · 2020Article
- Mechanical Deformation and Electronic Structure of a Blue Copper Azurin in a Solid-State Junction.Biomolecules · 2019Article
- Hole Hopping Across a Protein-Protein Interface.The journal of physical chemistry. B · 2019Article
- The Periodic Table's Impact on Bioinorganic Chemistry and Biology's Selective Use of Metal Ions.Structure and bonding · 2019Article
- Fluctuating hydrogen-bond networks govern anomalous electron transfer kinetics in a blue copper protein.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Prediction of Reduction Potentials of Copper Proteins with Continuum Electrostatics and Density Functional Theory.Chemistry (Weinheim an der Bergstrasse, Germany) · 2017Article
- Computational evidence support the hypothesis of neuroglobin also acting as an electron transfer species.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Article
- Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.Biochimica et biophysica acta · 2016Review
- Article
- Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.Chemical reviews · 2014Review
- Protein design: toward functional metalloenzymes.Chemical reviews · 2014Review
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5 authors.
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Abstract
Low reorganization free energies are necessary for fast electron transfer (ET) reactions. Hence, rational design of redox proteins with lower reorganization free energies has been a long-standing challenge, promising to yield a deeper understanding of the underlying principles of ET reactivity and to enable potential applications in different energy conversion systems. Herein we report studies of the intramolecular ET from pulse radiolytically produced disulfide radicals to Cu(II) in rationally designed azurin mutants. In these mutants, the copper coordination sphere has been fine-tuned to span a wide range of reduction potentials while leaving the metal binding site effectively undisrupted. We find that the reorganization free energies of ET within the mutants are indeed lower than that of WT azurin, increasing the intramolecular ET rate constants almost 10-fold: changes that are correlated with increased flexibility of their copper sites. Moreover, the lower reorganization free energy results in the ET rate constants reaching a maximum value at higher driving forces, as predicted by the Marcus theory.
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