Conformational control over proton-coupled electron transfer in metalloenzymes.

Nat Rev Chem

Department of Chemistry, College of Liberal Arts and Sciences, University of Illinois Urbana-Champaign, Urbana, IL, USA.

Published: October 2024

AI Article Synopsis

  • Metalloenzymes play a crucial role in important chemical transformations, impacting global geochemical and biochemical cycles, such as reducing dinitrogen and oxidizing water.
  • These reactions are complex and require precise coordination of electrons and protons, often involving protein structural rearrangements that dictate their rates.
  • The study focuses on specific metalloenzymes like nitrogenase, photosystem II, and ribonucleotide reductase, highlighting how structural changes influence their electronic properties and overall function.

Article 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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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11531298PMC
http://dx.doi.org/10.1038/s41570-024-00646-7DOI Listing

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