Resonance Raman Spectroscopy of the Neutral Radical Trp306 in DNA Photolyase
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.
MSU Digital Commons Citation
Gurudas, Ullas and Schelvis, Johannes, "Resonance Raman Spectroscopy of the Neutral Radical Trp306 in DNA Photolyase" (2004). Department of Chemistry and Biochemistry Faculty Scholarship and Creative Works. 386.