ReviewNature reviews. Chemistry2024
Conformational control over proton-coupled electron transfer in metalloenzymes.
Review in Nature reviews. Chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Engineering an Artificial Metalloenzyme for Efficient Photo-Enzymatic COAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Low-barrier hydrogen bond powers long-range radical transfer in the metal-free ribonucleotide reductase.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Biomimetic Fermentation Reshapes Precursor Pools to Drive Synergistic Roasting Reactions and Enhance Coffee Flavor Complexity.Foods (Basel, Switzerland) · 2026Article
- Thermodynamic and Kinetic Analysis of Galactose Oxidase Direct Electron Transfer on Carboxyl-Terminated SAM-Modified Gold Electrodes.Molecules (Basel, Switzerland) · 2026Article
- Proton transfer during reduction of the catalytic metallo-cofactors of the three nitrogenase isozymes.Chemical science · 2025Article
- Pursuing spatiotemporal coordination in electrocatalysis.Nature reviews. Chemistry · 2025Article
- Conformation-Dependent Hydrogen-Bonding Interactions in a Switchable Artificial Metalloprotein.Biochemistry · 2024Article
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Authors and funding
2 authors.
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Abstract
From the reduction of dinitrogen to the oxidation of water, the chemical transformations catalysed by metalloenzymes underlie global geochemical and biochemical cycles. These reactions represent some of the most kinetically and thermodynamically challenging processes known and require the complex choreography of the fundamental building blocks of nature, electrons and protons, to be carried out with utmost precision and accuracy. The rate-determining step of catalysis in many metalloenzymes consists of a protein structural rearrangement, suggesting that nature has evolved to leverage macroscopic changes in protein molecular structure to control subatomic changes in metallocofactor electronic structure. The proton-coupled electron transfer mechanisms operative in nitrogenase, photosystem II and ribonucleotide reductase exemplify this interplay between molecular and electronic structural control. We present the culmination of decades of study on each of these systems and clarify what is known regarding the interplay between structural changes and functional outcomes in these metalloenzyme linchpins.
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