comparative studies on picosecond-resolved fluorescence of D-amino acid oxidases from human with one from porcine kidney. Photoinduced electron transfer from aromatic amino acids to the excited flavin
comparative studies on picosecond-resolved fluorescence of D-amino acid oxidases from human with one from porcine kidney. Photoinduced electron transfer from aromatic amino acids to the excited flavin
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人 D-氨基酸氧化酶与猪肾 D-氨基酸氧化酶皮秒分辨荧光的比较研究。
DOI：
10.1016/j.jphotobiol.2019.111546
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发表时间：
2019
期刊：
影响因子：
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通讯作者：
Sirirat Kokpol
中科院分区：
文献类型：
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作者：
Seiji Taniguchi;Haik Chosrowjan;Syoji Ito;Hiroshi Miyasaka Masumi Katane;Hiroshi Homma;Fumio Tanaka;Arthit Nueangaudom;Kiattisak Lugsanangarm;Sirirat Kokpol
在皮秒时域内研究了人-氨基酸氧化酶（hDAAO）及其五种抑制剂的荧光动力学，并与已报道的猪肾吲哚-氨基酸氧化酶（pkDAAO）进行了比较。荧光寿命在二聚体中为47 ps，在单体中为235 ps，与pkDAAO的荧光寿命（45 ps-185 ps）进行了比较。hDAAO的荧光寿命在抑制剂结合后没有改变，尽管在吸收光谱中的修改。这表明配合物的寿命太短，无法用皮秒寿命仪器检测。芳香族氨基酸的数量在两种DAAO之间是相似的。利用晶体结构用ET理论分析了hDAAO的荧光寿命。二聚体和单体的寿命差异在两种形式的蛋白质之间激发的异咯嗪（Iso*）的电子亲和力差异方面得到了很好的描述，尽管尚不清楚单体的结构是否与二聚体不同。三个最快的ET供体是二聚体中的Tyr 314、Trp 52和Tyr 224，而单体中的Tyr 314、Tyr 224和Tyr 55，与二聚体中的Tyr 314、Tyr 224和Tyr 228以及单体中的Tyr 224、Tyr 314和Tyr 228相比。hDAAO二聚体中Trp 55的ET速率比pkDAAO二聚体中的速率快得多。在hDAAO中未观察到具有负指前因子的上升分量，而在pkDAAO中观察到。
Fluorescence dynamics of humand-amino acid oxidase (hDAAO) and its five inhibitors have been studied in the picoseconds time domain, and compared with one ind-amino acid oxidase from porcine kidney (pkDAAO) reported. The fluorescence lifetimes were identified as 47 ps in the dimer, 235 ps in the monomer, which are compared with those of pkDAAO (45 ps–185 ps). The fluorescence lifetimes of the hDAAO did not change upon the inhibitor bindings despite of modifications in the absorption spectra. This indicates that the lifetimes of the complexes are too short to detect with the picosecond lifetime instrument. Numbers of the aromatic amino acids are similar between the both DAAOs. The fluorescence lifetimes of hDAAO were analysed with an ET theory using the crystal structure. The difference in the lifetimes of the dimer and monomer was well described in terms of difference in the electron affinity of the excited isoalloxazine (Iso*) between the two forms of the protein, though it is not known whether the structure of the monomer is different from the dimer. Three fastest ET donors were Tyr314, Trp52 and Tyr224 in the dimer, while Tyr314, Tyr224 and Tyr55 in the monomer, which are compared to those in pkDAAO, Tyr314, Tyr224 and Tyr228 in the dimer, and Tyr224, Tyr314 and Tyr228 in the monomer. The ET rate from Trp55 in hDAAO dimer was much faster compared to the rate in pkDAAO dimer. A rise component with negative pre-exponential factor was not observed in hDAAO, which are found in pkDAAO.