Intramolecular and intermolecular perturbation on electronic state of FAD free in solution and bound to flavoproteins: FTIR spectroscopic study by using the C = O stretching vibrations as probes.
Intramolecular and intermolecular perturbation on electronic state of FAD free in solution and bound to flavoproteins: FTIR spectroscopic study by using the C = O stretching vibrations as probes.
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溶液中游离 FAD 和与黄素蛋白结合的 FAD 电子态的分子内和分子间扰动：使用 C = O 伸缩振动作为探针进行 FTIR 光谱研究。
DOI：
10.1093/jb/mvm129
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发表时间：
2007
影响因子：
2.7
通讯作者：
K. Shiga
中科院分区：
文献类型：
--
作者：
Y. Nishina;Kyosuke Sato;C. Setoyama;H. Tamaoki;R. Miura;K. Shiga
在D(2)O溶液中，以C=O拉伸振动为探针，利用FTIR光谱研究了FAD分子内和分子间的电子态扰动。用2-(13)C、（18）O=C(2)或4,10a-(13)C(2)标记的8-CN-、8-Cl-、8-H-、8-OCH(3)-和8-NH(2)- fad进行波段分配。8位取代使氧化态FAD的C(2)=O和C(4)=O伸展振动发生系统位移，即取代基的给电子能力(nh2 (2) > OCH（3) > CH(3) > H > Cl > CN）越强，出现C(2)=O和C(4)=O能带的波数区域越低。而阴离子还原FAD的C(4)=O带几乎没有移位。含有C(2)=O拉伸振动的1645 cm（-1）带在中链酰基辅酶a脱氢酶（MCAD）结合状态下转移到1630 cm(-1)，这可以通过黄素环C(2)=O处的氢键来解释。在MCAD与3-硫代辛烷酰辅酶a复合物的1,607 cm（-1）处观察到条带。氧化黄素与阴离子酰基辅酶a之间的电荷转移相互作用解释了23 cm（-1）的位移。以电子转移型黄蛋白为例，在1712 cm和1686 cm（-1）处获得了两条与C(4)=O拉伸振动相关的条带，为该蛋白的多重构象提供了证据。
The intramolecular and intermolecular perturbation on the electronic state of FAD was investigated by FTIR spectroscopy by using the C=O stretching vibrations as probes in D(2)O solution. Natural and artificial FADs, i.e. 8-CN-, 8-Cl-, 8-H-, 8-OCH(3)-, and 8-NH(2)-FAD labelled by 2-(13)C, (18)O=C(2), or 4,10a-(13)C(2) were used for band assignments. The C(2)=O and C(4)=O stretching vibrations of oxidized FAD were shifted systematically by the substitution at the 8-position, i.e. the stronger the electron-donating ability (NH(2) > OCH(3) > CH(3) > H > Cl > CN) of the substituent, the lower the wavenumber region where both the C(2)=O and C(4)=O bands appear. In contrast, the C(4)=O band of anionic reduced FAD scarcely shifted. The 1,645-cm(-1) band containing C(2)=O stretching vibration shifted to 1,630 cm(-1) in the medium-chain acyl-CoA dehydrogenase (MCAD)-bound state, which can be explained by hydrogen bonds at C(2)=O of the flavin ring. The band was observed at 1,607 cm(-1) in the complex of MCAD with 3-thiaoctanoyl-CoA. The 23 cm(-1) shift was explained by the charge-transfer interaction between oxidized flavin and the anionic acyl-CoA. In the case of electron-transferring flavoprotein, two bands associated with the C(4)=O stretching vibration were obtained at 1,712 and 1,686 cm(-1), providing evidence for the multiple conformations of the protein.
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DOI：
10.1073/pnas.90.16.7523
发表时间：
1993-08-15
影响因子：
11.1
作者：
KIM, JJP;WANG, M;PASCHKE, R
通讯作者：
PASCHKE, R
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影响因子：
2.9
作者：
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通讯作者：
Massey,V
DOI：
10.1073/pnas.93.25.14355
发表时间：
1996-12-10
影响因子：
11.1
作者：
Roberts, DL;Frerman, FE;Kim, JJP
通讯作者：
Kim, JJP
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影响因子：
2.9
作者：
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通讯作者：
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影响因子：
2.9
作者：
Lau,SM;Powell,P;Buettner,H;Ghisla,S;Thorpe,C
通讯作者：
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