Describing two-photon absorptivity of fluorescent proteins with a new vibronic coupling mechanism.
Describing two-photon absorptivity of fluorescent proteins with a new vibronic coupling mechanism.
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DOI:
10.1021/jp211020k
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发表时间:
2012-02-09
影响因子:
3.3
通讯作者:
Rebane, A.
中科院分区:
文献类型:
--
作者:
Drobizhev, M.;Makarov, N. S.;Tillo, S. E.;Hughes, T. E.;Rebane, A.
Fluorescent proteins (FPs) are widely used in two-photon microscopy as genetically-encoded probes. Understanding the physical basics of their two-photon absorption (2PA) properties is therefore crucial for creation of two-photon brighter mutants. On the other hand, it can give us better insight into molecular interactions of the FP chromophore with complex protein environment. It is known that, compared to one-photon absorption spectrum, where the pure electronic transition is the strongest, the 2PA spectrum of a number of FPs is dominated by a vibronic transition. The physical mechanism of such intensity redistribution is not understood. Here we present a new physical model that explains this effect through the “Herzberg-Teller”-type vibronic coupling of the difference between the permanent dipole moments in the ground and excited states (Δμ) to the bond-length-alternating coordinate. This model also enables us to quantitatively describe a large variability of the 2PA peak intensity in a series of red FPs with the same chromophore through the interference between the “Herzberg-Teller” and Franck-Condon terms.
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