Resonance Raman spectroscopy of the neutral radical Trp306 in DNA photolyase

Ullas Gurudas; Johannes P.M. Schelvis

doi:10.1021/ja047161d

Resonance Raman spectroscopy of the neutral radical Trp₃₀₆ in DNA photolyase

Ullas Gurudas, Johannes P.M. Schelvis

Chemistry and Biochemistry

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

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
DOIs	https://doi.org/10.1021/ja047161d
State	Published - 13 Oct 2004

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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.",

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AU - Schelvis, Johannes P.M.

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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.

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Resonance Raman spectroscopy of the neutral radical Trp₃₀₆ in DNA photolyase

Abstract

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