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A tyrosine–tryptophan dyad and radical-based charge transfer in a ribonucleotide reductase-inspired maquette

Author

Listed:
  • Cynthia V. Pagba

    (School of Chemistry and Biochemistry, Georgia Institute of Technology
    Parker H. Petit Institute of Bioengineering and Bioscience, Georgia Institute of Technology)

  • Tyler G. McCaslin

    (School of Chemistry and Biochemistry, Georgia Institute of Technology
    Parker H. Petit Institute of Bioengineering and Bioscience, Georgia Institute of Technology)

  • Gianluigi Veglia

    (Biophysics and Molecular Biology, University of Minnesota
    University of Minnesota)

  • Fernando Porcelli

    (Biophysics and Molecular Biology, University of Minnesota
    University of Minnesota
    Agro-food and Forest Systems, University of Tuscia)

  • Jiby Yohannan

    (School of Chemistry and Biochemistry, Georgia Institute of Technology
    Parker H. Petit Institute of Bioengineering and Bioscience, Georgia Institute of Technology)

  • Zhanjun Guo

    (School of Chemistry and Biochemistry, Georgia Institute of Technology
    Parker H. Petit Institute of Bioengineering and Bioscience, Georgia Institute of Technology)

  • Miranda McDaniel

    (School of Chemistry and Biochemistry, Georgia Institute of Technology
    Parker H. Petit Institute of Bioengineering and Bioscience, Georgia Institute of Technology)

  • Bridgette A. Barry

    (School of Chemistry and Biochemistry, Georgia Institute of Technology
    Parker H. Petit Institute of Bioengineering and Bioscience, Georgia Institute of Technology)

Abstract

In class 1a ribonucleotide reductase (RNR), a substrate-based radical is generated in the α2 subunit by long-distance electron transfer involving an essential tyrosyl radical (Y122O·) in the β2 subunit. The conserved W48 β2 is ∼10 Å from Y122OH; mutations at W48 inactivate RNR. Here, we design a beta hairpin peptide, which contains such an interacting tyrosine–tryptophan dyad. The NMR structure of the peptide establishes that there is no direct hydrogen bond between the phenol and the indole rings. However, electronic coupling between the tyrosine and tryptophan occurs in the peptide. In addition, downshifted ultraviolet resonance Raman (UVRR) frequencies are observed for the radical state, reproducing spectral downshifts observed for β2. The frequency downshifts of the ring and CO bands are consistent with charge transfer from YO· to W or another residue. Such a charge transfer mechanism implies a role for the β2 Y-W dyad in electron transfer.

Suggested Citation

  • Cynthia V. Pagba & Tyler G. McCaslin & Gianluigi Veglia & Fernando Porcelli & Jiby Yohannan & Zhanjun Guo & Miranda McDaniel & Bridgette A. Barry, 2015. "A tyrosine–tryptophan dyad and radical-based charge transfer in a ribonucleotide reductase-inspired maquette," Nature Communications, Nature, vol. 6(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms10010
    DOI: 10.1038/ncomms10010
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