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 |
|---|---|
| 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 |
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Resonance Raman spectroscopy of the neutral radical Trp306 in DNA photolyase. / Gurudas, Ullas; Schelvis, Johannes.
In: Journal of the American Chemical Society, Vol. 126, No. 40, 13.10.2004, p. 12788-12789.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - Resonance Raman spectroscopy of the neutral radical Trp306 in DNA photolyase
AU - Gurudas, Ullas
AU - Schelvis, Johannes
PY - 2004/10/13
Y1 - 2004/10/13
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=5644261208&partnerID=8YFLogxK
M3 - Article
VL - 126
SP - 12788
EP - 12789
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 40
ER -