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Gas-phase absorption properties of DsRed model chromophores

机译：DsRed模型发色团的气相吸收特性

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The absorption spectra of two compounds, RFP(1) and RFP(2), designed to model the chromophore of the Red Fluorescent Protein DsRed have been recorded in the gas phase with a heavy-ion storage ring technique. Both anions and cations were investigated. The electronic delocalization is greater in RFP(2) than in RFP(1) due to an additional CC double bond in conjugation with the p system, and the absorption bands of RFP(2) are red-shifted compared to those of RFP(1). Band maxima of the RFP(2) and RFP(1) anions are 549 nm and 521 nm, respectively, and of the cations 448 nm and 441 nm, respectively. These values are in good agreement with calculated HOMO-LUMO gaps at the B3LYP/6-311++G(2d,p)//PM3 level of theory: 559 nm and 496 nm for the RFP(2) and RFP(1) anions and 452 nm and 436 nm for the corresponding cations. The protein absorbs maximally at 558 nm and it is assumed that the chromophore is anionic. Hence, the electronic structure of the RFP(2) anion is close to that of the in vivo chromophore in its protein environment. A comparison is made between the two model chromophores and their well-known Green Fluorescent Protein homologue chromophore, as well as between different media (gas phase, solution phase). For the anionic gas-phase spectra, vibrational structures are clearly resolved for both compounds (hnu(0) = 382 +/- 10 cm(-1) for RFP(1) and 518 +/- 10 cm(-1) for RFP(2)) and are assigned to harmonic vibrational progressions due to collective motion of the entire chromophores. Based on calculations on model chromophores closer to the wild-type DsRed chromophore, we suggest that the protein environment forces the chromophore to adopt a planar geometry. [References: 23]
机译：采用重离子存储环技术已在气相中记录了两种化合物RFP（1）和RFP（2）的吸收光谱，这些化合物旨在模拟红色荧光蛋白DsRed的发色团。研究了阴离子和阳离子。 RFP（2）中的电子离域比RFP（1）中大，这是因为与p系统共轭了一个额外的CC双键，与RFP（1）相比，RFP（2）的吸收带发生了红移。 ）。 RFP（2）和RFP（1）阴离子的谱带最大值分别为549 nm和521 nm，阳离子的谱带最大值分别为448 nm和441 nm。这些值与在理论水平的B3LYP / 6-311 ++ G（2d，p）// PM3处计算出的HOMO-LUMO间隙非常一致：RFP（2）和RFP（1）的559 nm和496 nm分别为452 nm和436 nm。该蛋白质在558 nm处最大吸收，并且假定发色团是阴离子的。因此，RFP（2）阴离子的电子结构接近其蛋白质环境中的体内发色团的电子结构。比较了两种模型发色团及其众所周知的绿色荧光蛋白同源发色团以及不同介质（气相，溶液相）之间的比较。对于阴离子气相光谱，两种化合物的振动结构均得到清晰解析（对于RFP（1），hnu（0）= 382 +/- 10 cm（-1）;对于RFP，518 +/- 10 cm（-1） （2））和归因于整个生色团的集体运动而引起的谐波振动级数。基于对更接近野生型DsRed生色团的模型生色团的计算，我们建议蛋白质环境迫使生色团采用平面几何形状。 [参考：23]

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