Resonance Raman spectroscopy of the neutral radical Trp306 in DNA photolyase

Ullas Gurudas, Johannes Schelvis

Research output: Contribution to journalArticle

13 Citations (Scopus)

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 languageEnglish
Pages (from-to)12788-12789
Number of pages2
JournalJournal of the American Chemical Society
Volume126
Issue number40
StatePublished - 13 Oct 2004

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Deoxyribodipyrimidine Photo-Lyase
Raman Spectrum Analysis
Raman spectroscopy
DNA
Proteins
Escherichia coli Proteins
Vibration
Tryptophan
Escherichia coli
Raman scattering
Electrons

Cite this

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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 journalArticle

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