Proton transfer and structure-specific fluorescence in hydrogen bond-rich protein structures. Pinotsi, D., Grisanti, L., Mahou, P., Gebauer, R., Kaminski, C., F., Hassanali, A., A., & Kaminski Schierle, G., S. Journal of the American Chemical Society, 138(9):3046-3057, American Chemical Society, 1, 2016. Paper Website abstract bibtex Protein structures which form fibrils have recently been shown to absorb light at energies in the near UV range and to exhibit a structure-specific fluorescence in the visible range even in the absence of aromatic amino acids. However, the molecular origin of this phenomenon has so far remained elusive. Here, we combine ab initio molecular dynamics simulations and fluorescence spectroscopy to demonstrate that these intrinsically fluorescent protein fibrils are permissive to proton transfer across hydrogen bonds which can lower electron excitation energies and thereby decrease the likelihood of energy dissipation associated with conventional hydrogen bonds. The importance of proton transfer on the intrinsic fluorescence observed in protein fibrils is signified by large reductions in the fluorescence intensity upon either fully protonating, or deprotonating, the fibrils at pH=0 or pH=14, respectively. Thus, our results point to the existence of a structure-specific fluorophore that does not require the presence of aromatic residues or multiple bond conjugation that characterise conventional fluorescent systems. The phenomenon may have a wide range of implications in biological systems and in the design of self-assembled functional materials.
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title = {Proton transfer and structure-specific fluorescence in hydrogen bond-rich protein structures.},
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abstract = {Protein structures which form fibrils have recently been shown to absorb light at energies in the near UV range and to exhibit a structure-specific fluorescence in the visible range even in the absence of aromatic amino acids. However, the molecular origin of this phenomenon has so far remained elusive. Here, we combine ab initio molecular dynamics simulations and fluorescence spectroscopy to demonstrate that these intrinsically fluorescent protein fibrils are permissive to proton transfer across hydrogen bonds which can lower electron excitation energies and thereby decrease the likelihood of energy dissipation associated with conventional hydrogen bonds. The importance of proton transfer on the intrinsic fluorescence observed in protein fibrils is signified by large reductions in the fluorescence intensity upon either fully protonating, or deprotonating, the fibrils at pH=0 or pH=14, respectively. Thus, our results point to the existence of a structure-specific fluorophore that does not require the presence of aromatic residues or multiple bond conjugation that characterise conventional fluorescent systems. The phenomenon may have a wide range of implications in biological systems and in the design of self-assembled functional materials.},
bibtype = {article},
author = {Pinotsi, Dorothea and Grisanti, Luca and Mahou, Pierre and Gebauer, Ralph and Kaminski, Clemens F. and Hassanali, Ali A and Kaminski Schierle, Gabriele S.},
journal = {Journal of the American Chemical Society},
number = {9}
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