Gurudas Ullas, Schelvis Johannes P M
Department of Chemistry, New York University, 100 Washington Square East, Room 1001, New York, NY 10003, USA.
J Am Chem Soc. 2004 Oct 13;126(40):12788-9. doi: 10.1021/ja047161d.
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.
