Abstract
Recently, we have reported the use of near-infrared (NIR) Yb3+ vibronic sideband (VSB) spectroscopy to obtain structural information of metal-binding sites in proteins (1). In the NIR fluorescence spectrum of metalloproteins where Yb3+ is reconstituted into the metal binding site, weak vibronic sidebands that are shifted in energy with respect to the principal Yb3+ 2F5/2 -> 2F7/2 zero-phonon electronic transition (at ca. 970 nm), correspond to the vibrational frequencies of the Yb3+ ligands. This Yb3+ VSB spectrum provides a selective well-resolved “infrared-like” vibrational spectrum of the ligands which constitute the metal binding site.
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References
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Roselli, C., Boussac, A., Mattioli, T.A. (1995). Near Infrared Yb3+ Vibronic Sideband Spectroscopy of Proteins: Amino-Acid Side Chain Models. In: Merlin, J.C., Turrell, S., Huvenne, J.P. (eds) Spectroscopy of Biological Molecules. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-0371-8_36
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DOI: https://doi.org/10.1007/978-94-011-0371-8_36
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