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

Cynthia V. Pagba, Tyler G. McCaslin, Gianluigi Veglia, Fernando Porcelli, Jiby Yohannan, Zhanjun Guo, Miranda McDaniel and Bridgette A. Barry ()
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Cynthia V. Pagba: School of Chemistry and Biochemistry, Georgia Institute of Technology
Tyler G. McCaslin: School of Chemistry and Biochemistry, Georgia Institute of Technology
Gianluigi Veglia: Biophysics and Molecular Biology, University of Minnesota
Fernando Porcelli: Biophysics and Molecular Biology, University of Minnesota
Jiby Yohannan: School of Chemistry and Biochemistry, Georgia Institute of Technology
Zhanjun Guo: School of Chemistry and Biochemistry, Georgia Institute of Technology
Miranda McDaniel: School of Chemistry and Biochemistry, Georgia Institute of Technology
Bridgette A. Barry: School of Chemistry and Biochemistry, Georgia Institute of Technology

Nature Communications, 2015, vol. 6, issue 1, 1-8

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms10010

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