Resonance enhancement of two-photon absorption in fluorescent proteins
Resonance enhancement of two-photon absorption in fluorescent proteins
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DOI：
10.1021/jp075879k
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发表时间：
2007-12-20
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.;Rebane, A.
我们测量了野生型绿色荧光蛋白、青色荧光蛋白和单体红色荧光蛋白在宽光谱范围（λ (2PA) = 550 ~ 1300 nm）的绝对横截面值的双光子吸收（2PA）光谱，并首次在我们所知的短波长区域发现了一个新的S-0 -> S-n 2PA跃迁。这种转变被强烈地共振增强，显示出类似于20-160 GM的2PA横截面值，比相应蛋白质的最低能量（S-0 -> S-1）转变所测得的值至少高2-4倍。我们还证明了从2PA截面可以推导出S-0 -> S-1激励下的永久偶极矩（垂杆δ mu（10）垂杆）的变化，为快速评估生理条件下的垂杆δ mu（10）垂杆提供了一种新的工具。
We measure two-photon absorption (2PA) spectra of wild-type green fluorescent protein, cyan fluorescent protein, and monomeric red fluorescent protein in absolute cross section values in a wide spectral range (lambda(2PA) = 550 - 1300 nm), and find, for the first time to our knowledge, a new S-0 -> S-n 2PA transition in all three proteins in the short-wavelength region. This transition is strongly resonantly enhanced, showing 2PA cross section values of similar to 20-160 GM, which are at least 2-4 times higher than those measured in the lowest energy (S-0 -> S-1) transition of corresponding proteins. We also show that the change of permanent dipole moment upon S-0 -> S-1 excitation (vertical bar Delta mu(10)vertical bar) can be deduced from 2PA cross section, providing a new tool for fast evaluation of vertical bar Delta mu(10)vertical bar in physiological conditions.