Two-Photon Excitation of Flavins and Flavoproteins with Classical and Quantum Light.
Two-Photon Excitation of Flavins and Flavoproteins with Classical and Quantum Light.
复制标题
用经典光和量子光双光子激发黄素和黄素蛋白。
DOI：
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发表时间：
2018
影响因子：
15
通讯作者：
T. Goodson
中科院分区：
文献类型：
--
作者：
Juan P. Villabona;O. Varnavski;B. Palfey;T. Goodson
在这项贡献中，研究了天然黄素蛋白的纠缠双光子吸收(ETPA)过程。研究了在蛋白质环境中嵌入黄素单核苷酸(FMN)和黄素腺嘌呤二核苷酸(FAD)发色团的低温反应蛋白(LOT6P)和b型二氢罗酸脱氢酶(DHOD B)。我们测量了ETPA截面，发现当从游离黄素生色团的水溶液到嵌入蛋白质的生色团时，ETPA截面增大。与经典光相比，当纠缠光子用作激发光时，这种增强尤为明显。我们的结果证明了ETPA作为荧光蛋白传感技术的潜力，即使对于那些经典的TPA横截面与众所周知的荧光蛋白相比很小的情况下也是如此。
In this contribution, the entangled two-photon absorption (ETPA) process on naturally occurring flavoproteins was studied. Low temperature responsive protein (LOT6P) and b-type dihydroorotate dehydrogenase (DHOD B), which possess flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD) chromophores embedded in the protein environment, were investigated. The ETPA cross-section was measured, and we found that it increases when going from an aqueous solution of the free flavin chromophore to the chromophore embedded in the protein. This enhancement is particularly evident when entangled photons are used as excitation light compared to classical light. Our results prove the potential of ETPA as a sensing technique for fluorescent proteins even for those whose classical TPA cross-section is small compared to well-known fluorescent proteins.
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影响因子：
56.9
作者：
PARK, HW;KIM, ST;DEISENHOFER, J
通讯作者：
DEISENHOFER, J
影响因子：
15
作者：
Kao, Ya-Ting;Saxena, Chaitanya;He, Ting-Fang;Guo, Lijun;Wang, Lijuan;Sancar, Aziz;Zhong, Dongping
通讯作者：
Zhong, Dongping
影响因子：
14.9
作者：
Rose AS;Hildebrand PW
通讯作者：
Hildebrand PW
DOI：
10.1073/pnas.93.20.10763
发表时间：
1996-10-01
影响因子：
11.1
作者：
Xu, C;Zipfel, W;Webb, WW
通讯作者：
Webb, WW