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.
Gurudas
Ullas
U
Department of Chemistry, New York University, 100 Washington Square East, Room 1001, New York, NY 10003, USA.
Schelvis
Johannes P M
JP
D004255:Deoxyribodipyrimidine Photo-Lyase / Q000737:chemistry* / Q000378:metabolism; D005182:Flavin-Adenine Dinucleotide / Q000737:chemistry; D005609:Free Radicals / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D010777:Photochemistry; D013059:Spectrum Analysis, Raman; D014364:Tryptophan / Q000737:chemistry*
D005609:Free Radicals; D005182:Flavin-Adenine Dinucleotide; D014364:Tryptophan; D004255:Deoxyribodipyrimidine Photo-Lyase