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Related Experiment Videos

Density functional calculations on model tyrosyl radicals

F Himo1, A Gräslund, L A Eriksson

  • 1Department of Physics, Arrhenius Laboratories, Stockholm University, Sweden.

Biophysical Journal
|April 1, 1997
PubMed
Summary
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This study confirms tyrosyl radicals in proteins are neutral using computational methods. Hydrogen bonding influences spin density, and radical orientation varies across different biological systems like photosystem II and ribonucleotide reductases.

Area of Science:

  • Computational chemistry
  • Biophysical chemistry
  • Quantum biology

Background:

  • Tyrosyl free radicals are crucial intermediates in biological processes, including charge transfer in photosystem II (PSII) and enzymatic reactions in ribonucleotide reductases (RNRs).
  • Understanding the electronic structure and hyperfine properties of these radicals is essential for elucidating their function.

Purpose of the Study:

  • To investigate the structure and hyperfine properties of model tyrosyl free radicals using advanced computational techniques.
  • To determine the charge state of tyrosyl radicals within protein environments.
  • To analyze the impact of hydrogen bonding on spin density distribution and radical conformation.

Main Methods:

  • Gradient-corrected density functional theory (DFT) with the PWP86 functional.

Related Experiment Videos

  • Application of large basis sets, specifically IGLO-III.
  • Comparison of calculated spin density distributions and proton hyperfine couplings with experimental data.

    • Main Results:

    • Calculations confirm that tyrosyl radicals in proteins are neutral.
    • Hydrogen bonding to the phenoxyl oxygen atom alters spin density, decreasing it on oxygen and increasing it on the C4 carbon.
    • Computed hyperfine coupling constants reveal distinct orientations of the alpha-carbon relative to the ring plane in different RNRs and PSII.

    Conclusions:

    • The study validates the neutral nature of protein-bound tyrosyl radicals.
    • Computational analysis provides insights into the structural and electronic effects of the protein environment on tyrosyl radicals.
    • Revised empirical parameters for experimental determination of spin densities are proposed based on these findings.