Abstract
The resonance Raman spectrum of the tryptophan neutral radical in a protein, Escherichia coli photolyase, is reported for the first time. The data compare very well to a solution study and computational predictions, and tentative assignments are made for the observed vibrations. This important new result demonstrates the potential of time-resolved resonance Raman spectroscopy as a powerful tool to investigate these radicals in protein electron-transfer processes and in enzymatic reactions in real time.
| Original language | English |
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| Pages (from-to) | 12788-12789 |
| Number of pages | 2 |
| Journal | Journal of the American Chemical Society |
| Volume | 126 |
| Issue number | 40 |
| State | Published - 13 Oct 2004 |