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Related Experiment Video

Updated: Jul 13, 2026

Line Shape Analysis of Dynamic NMR Spectra for Characterizing Coordination Sphere Rearrangements at a Chiral Rhenium Polyhydride Complex
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Buffer-assisted proton-coupled electron transfer in a model rhenium-tyrosine complex.

Hiroshi Ishikita1, Alexander V Soudackov, Sharon Hammes-Schiffer

  • 1Department of Chemistry, 104 Chemistry Building, Pennsylvania State University, University Park, Pennsylvania 16802, USA.

Journal of the American Chemical Society
|August 21, 2007
PubMed
Summary

Phosphate buffer, not water, facilitates tyrosyl radical generation via proton-coupled electron transfer (PCET) in a rhenium complex. This finding clarifies a key step in biologically important processes.

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The Synthesis, Characterization and Reactivity of a Series of Ruthenium N-triphosPh Complexes
10:51

The Synthesis, Characterization and Reactivity of a Series of Ruthenium N-triphosPh Complexes

Published on: April 10, 2015

Area of Science:

  • Inorganic Chemistry
  • Physical Chemistry
  • Biochemistry

Background:

  • Tyrosyl radical generation is crucial in many biological processes.
  • Understanding the mechanism of radical formation in organometallic complexes like [Re(P-Y)(phen)(CO)3]PF6 is essential.
  • Proton-coupled electron transfer (PCET) reactions are fundamental to chemical and biological transformations.

Purpose of the Study:

  • To elucidate the mechanism of tyrosyl radical generation in the [Re(P-Y)(phen)(CO)3]PF6 complex.
  • To investigate the role of different proton acceptors (water vs. phosphate buffer) in the PCET reaction.
  • To analyze the factors influencing the rate and kinetic isotope effect of the reaction.

Main Methods:

  • Multistate continuum theory was employed to model proton-coupled electron transfer (PCET) reactions.
  • Calculations considered both water and phosphate buffer species as potential proton acceptors.
  • Analysis included reorganization energies, reaction free energies, activation free energies, and vibronic couplings for hydrogen and deuterium transfer.

Main Results:

  • The phosphate buffer species HPO4(2-) was identified as the effective proton acceptor, successfully reproducing experimental pH dependence and H/D kinetic isotope effects.
  • A model using water as the proton acceptor was found to be physically unreasonable for this system.
  • The dominant rate contributions arise from nonadiabatic transitions to higher product vibronic states due to larger vibronic coupling and overlap.

Conclusions:

  • Phosphate buffer species, specifically HPO4(2-), play a critical role in the tyrosyl radical generation mechanism of the studied rhenium complex.
  • The smaller proton donor-acceptor distance and favorable electronic interactions make phosphate a more effective proton acceptor than water.
  • The findings provide fundamental insights into tyrosyl radical generation, relevant to various biological systems.