Remarkably, the long-timescale fluorescence may then be regarded as a side
channel [19, 71] only enabled in the absence of relevant electron acceptors.
References
1. Tsien, R.Y.: The green fluorescent protein. Annu. Rev. Biochem. 67, 509–544 (1998)
2. Ormo ¨, M., Cubitt, A.B.., Kallio, K., Gross, L.A., Tsien, R.Y., Remington, S.J.: Crystal
structure of the Aequorea victoria green fluorescent protein. Science 273, 1392–1395 (1996)
3. Yang, F., Moss, L.G., Phillips, G.N.: The molecular structure of green fluorescent protein. Nat.
Biotechnol. 14, 1246–1251 (1996)
4. Chudakov, D., Matz, M., Lukyanov, S., Lukyanov, K.: Fluorescent proteins and their
applications in imaging living cells and tissues. Physiol. Rev. 90, 1103–1163 (2010)
5. Tolbert, L.M., Baldridge, A., Kowalik, J., Solntsev, K.M.: Collapse and recovery of green
fluorescent protein chromophore emission through topological effects. Acc. Chem. Res. 45,
171–181 (2012)
6. Chattoraj, M., King, B., Bublitz, G., Boxer, S.: Ultra-fast excited state dynamics in green
fluorescent protein: multiple states and proton transfer. Proc. Natl Acad. Sci. USA 93,
8362–8367 (1996)
7. Fang, C., Frontiera, R.R., Tran, R., Mathies, R.A.: Mapping GFP structure evolution during
proton transfer with femtosecond Raman spectroscopy. Nature 462, 200–204 (2009)
8. Sample, V., Newman, R.H., Zhang, J.: The structure and function of fluorescent proteins.
Chem. Soc. Rev. 38, 2852–2864 (2009)
9. Shcherbo, D., Shemiakina, I., Ryabova, A., Luker, K., Schmidt, B., Souslova, E.,
Gorodnicheva, T., Strukova, L., Shidlovskiy, K., Britanova, O., Zaraisky, A., Lukyanov, K.,
Loschenov, V., Luker, G., Chudakov, D.: Near-infrared fluorescent proteins. Nat. Methods 7,
827–829 (2010)
10. Forbes, M.W., Jockusch, R.A.: Deactivation pathways of an isolated green fluorescent protein
model chromophore studied by electronic action spectroscopy. J. Am. Chem. Soc. 131,
17038–17039 (2009)
11. Toniolo, A., Olsen, S., Manoha, L., Martinez, T.J.: Conical intersection dynamics in solution:
the chromophore of green fluorescent protein. Faraday Discuss. 127, 149–163 (2004)
12. Martin, M.E., Negri, F., Olivucci, M.: Origin, nature, and fate of the fluorescent state of the
green fluorescent protein chromophore at the CASPT2//CASSCF resolution. J. Am. Chem.
Soc. 126, 5452–5464 (2004)
13. Polyakov, I.V., Grigorenko, B.L., Epifanovsky, E.M., Krylov, A.I., Nemukhin, A.V.: Potential
energy landscape of the electronic states of the GFP chromophore in different protonation
forms: electronic transition energies and conical intersections. J. Chem. Theory Comput. 6,
2377–2387 (2010)
14. Kummer, A., Kompa, C., Niwa, H., Hirano, T., Kojima, S., Michel-Beyerle, M.: Viscosity
dependent fluorescence decay of the GFP chromophore in solution due to fast internal
conversion. J. Phys. Chem. B 106, 7554–7559 (2002)
15. Mandal, D., Tahara, T., Meech, S.: Excited-state dynamics in the green fluorescent protein
chromophore. J. Phys. Chem. B 108, 1102–1108 (2004)
16. Gepshtein, R., Huppert, D., Agmon, N.: Deactivation mechanism of the green fluorescent
chromophore. J. Phys. Chem. B 110, 4434–4442 (2006)
17. Lukyanov, K.A., Chudakov, D.M., Lukyanov, S., Verkhusha, V.V.: Photoactivatable fluorescent proteins. Nat. Rev. Mol. Cell Biol. 6, 885–890 (2005)
18. Meech, S.R.: Excited state reactions in fluorescent proteins. Chem. Soc. Rev. 38, 2922–2934
(2009)
100
A.V. Bochenkova and L.H. Andersen
channel [19, 71] only enabled in the absence of relevant electron acceptors.
References
1. Tsien, R.Y.: The green fluorescent protein. Annu. Rev. Biochem. 67, 509–544 (1998)
2. Ormo ¨, M., Cubitt, A.B.., Kallio, K., Gross, L.A., Tsien, R.Y., Remington, S.J.: Crystal
structure of the Aequorea victoria green fluorescent protein. Science 273, 1392–1395 (1996)
3. Yang, F., Moss, L.G., Phillips, G.N.: The molecular structure of green fluorescent protein. Nat.
Biotechnol. 14, 1246–1251 (1996)
4. Chudakov, D., Matz, M., Lukyanov, S., Lukyanov, K.: Fluorescent proteins and their
applications in imaging living cells and tissues. Physiol. Rev. 90, 1103–1163 (2010)
5. Tolbert, L.M., Baldridge, A., Kowalik, J., Solntsev, K.M.: Collapse and recovery of green
fluorescent protein chromophore emission through topological effects. Acc. Chem. Res. 45,
171–181 (2012)
6. Chattoraj, M., King, B., Bublitz, G., Boxer, S.: Ultra-fast excited state dynamics in green
fluorescent protein: multiple states and proton transfer. Proc. Natl Acad. Sci. USA 93,
8362–8367 (1996)
7. Fang, C., Frontiera, R.R., Tran, R., Mathies, R.A.: Mapping GFP structure evolution during
proton transfer with femtosecond Raman spectroscopy. Nature 462, 200–204 (2009)
8. Sample, V., Newman, R.H., Zhang, J.: The structure and function of fluorescent proteins.
Chem. Soc. Rev. 38, 2852–2864 (2009)
9. Shcherbo, D., Shemiakina, I., Ryabova, A., Luker, K., Schmidt, B., Souslova, E.,
Gorodnicheva, T., Strukova, L., Shidlovskiy, K., Britanova, O., Zaraisky, A., Lukyanov, K.,
Loschenov, V., Luker, G., Chudakov, D.: Near-infrared fluorescent proteins. Nat. Methods 7,
827–829 (2010)
10. Forbes, M.W., Jockusch, R.A.: Deactivation pathways of an isolated green fluorescent protein
model chromophore studied by electronic action spectroscopy. J. Am. Chem. Soc. 131,
17038–17039 (2009)
11. Toniolo, A., Olsen, S., Manoha, L., Martinez, T.J.: Conical intersection dynamics in solution:
the chromophore of green fluorescent protein. Faraday Discuss. 127, 149–163 (2004)
12. Martin, M.E., Negri, F., Olivucci, M.: Origin, nature, and fate of the fluorescent state of the
green fluorescent protein chromophore at the CASPT2//CASSCF resolution. J. Am. Chem.
Soc. 126, 5452–5464 (2004)
13. Polyakov, I.V., Grigorenko, B.L., Epifanovsky, E.M., Krylov, A.I., Nemukhin, A.V.: Potential
energy landscape of the electronic states of the GFP chromophore in different protonation
forms: electronic transition energies and conical intersections. J. Chem. Theory Comput. 6,
2377–2387 (2010)
14. Kummer, A., Kompa, C., Niwa, H., Hirano, T., Kojima, S., Michel-Beyerle, M.: Viscosity
dependent fluorescence decay of the GFP chromophore in solution due to fast internal
conversion. J. Phys. Chem. B 106, 7554–7559 (2002)
15. Mandal, D., Tahara, T., Meech, S.: Excited-state dynamics in the green fluorescent protein
chromophore. J. Phys. Chem. B 108, 1102–1108 (2004)
16. Gepshtein, R., Huppert, D., Agmon, N.: Deactivation mechanism of the green fluorescent
chromophore. J. Phys. Chem. B 110, 4434–4442 (2006)
17. Lukyanov, K.A., Chudakov, D.M., Lukyanov, S., Verkhusha, V.V.: Photoactivatable fluorescent proteins. Nat. Rev. Mol. Cell Biol. 6, 885–890 (2005)
18. Meech, S.R.: Excited state reactions in fluorescent proteins. Chem. Soc. Rev. 38, 2922–2934
(2009)
100
A.V. Bochenkova and L.H. Andersen