Direct observation of a photoinduced radical pair in a cryptochrome blue-light photoreceptor.
Direct observation of a photoinduced radical pair in a cryptochrome blue-light photoreceptor.
复制标题
DOI：
10.1002/anie.200803102
复制
发表时间：
2009
影响因子：
16.6
通讯作者：
Weber, Stefan
中科院分区：
文献类型：
--
作者：
Biskup, Till;Schleicher, Erik;Okafuji, Asako;Link, Gerhard;Hitomi, Kenichi;Getzoff, Elizabeth D.;Weber, Stefan
来自光解酶/隐花色素家族的蛋白质共享它们的三维折叠、序列同源性和氧化还原活性黄素腺嘌呤二核苷酸(FAD)辅助因子，但表现出不同的活性。[1]它们对蓝光或UV-A光作出响应，在生理上参与DNA修复、生物钟夹带或其他过程。[1-3]光解酶/隐花色素家族的成员已被发现存在于从细菌到植物、动物和人类的各种生物中。[1]在这个家族中，最初从拟南芥和聚合胞中鉴定出的基因系统发育簇编码了类似于铬的蛋白质，它们不同于以前描述的“经典”植物(以拟南芥HY4为代表)或动物(以果蝇和智人为代表)的隐色素，但更接近后者。[4]值得注意的是，来自这个新的簇(Cry-dash)的隐色素现在已经在所有的生命王国中被发现。[5]虽然已经讨论了多种生物学功能，但来自不同物种的稳定、重组表达的Cry-dash蛋白的可用性为破译隐色素蛋白化学提供了手段。最近的实验结果表明，Cry-dash可以作为单链DNA的转录调节因子[4，5]和DNA修复酶发挥作用。[6]其他实验结果表明，Cry-dash参与了昼夜节律的输入途径。[7，8]氧化还原反应被认为在隐色素的光响应活动中发挥关键作用。体外和体内实验都表明，当采用信号转导状态时，Fad氧化还原状态从完全氧化(FADox)转变为自由基形式。结果与光解酶的氧化还原活性一致。[13]在后者中，当从FADOX开始时，光诱导电子转移(ET)产生由FAD和酪氨酸或色氨酸自由基组成的自由基对(RP)，可通过电子顺磁共振(EPR)直接观察到。
Proteins from the photolyase/cryptochrome family share their three-dimensional fold, sequence homology, and the redox-active flavin adenine dinucleotide (FAD) cofactor, but exhibit diverse activities.[1] In response to blue or UV-A light, they function physiologically in DNA repair, entrainment of the circadian clock, or other processes.[1-3] Members of the photolyase/cryptochrome family have been identified in various organisms ranging from bacteria to plants, animals and humans.[1] Within this family, a phylogenetic cluster of genes originally identified from Arabidopsis and Synechocystis encode cryptochrome-like proteins, which are distinct from previously characterized “classic” plant (represented by Arabidopsis HY4) or animal (represented by Drosophila and Homo sapiens) cryptochromes, yet more closely resemble the latter.[4] Remarkably, the cryptochromes from this new cluster (Cry-DASH) have now been found through all kingdoms of life.[5] While multiple biological functions have been discussed, the availability of stable, recombinantly expressed, Cry-DASH proteins from diverse species provides the means of deciphering cryptochrome protein chemistry. Results from recent experiments point to the direction that Cry-DASH could work as a transcriptional regulator,[4, 5] as well as a DNA repair enzyme for singlestranded DNA.[6] Other experimental results suggest the participation of Cry-DASH in circadian input pathways.[7, 8]Redox reactions are proposed to play a key role in light-responsive activities of cryptochromes.[9, 10] Both in vitro and in vivo experiments suggest that the FAD redox state is changed from fully oxidized (FADox) to the radical form when adopting the signaling state.[11, 12] The results agree with the redox activity of photolyases.[13] In the latter, when starting from FADox, photoinduced electron-transfer (ET) produces a radical pair (RP), comprised of an FAD and either a tyrosine or a tryptophan radical, directly observable by electron paramagnetic resonance (EPR).[14-16]
登录
查看更多内容
影响因子：
2.9
作者：
Brunelle, Stephanie A.;Hazard, E. Starr;Van Dolah, Frances M.
通讯作者：
Van Dolah, Frances M.
影响因子：
2.1
作者：
Daiyasu, H;Ishikawa, T;Toh, H
通讯作者：
Toh, H
影响因子：
3.4
作者：
Efimova, Olga;Hore, P. J.
通讯作者：
Hore, P. J.
影响因子：
15
作者：
Kay, CWM;Bittl, R;Weber, S
通讯作者：
Weber, S
影响因子：
4.8
作者：
Berndt, Alex;Kottke, Tilman;Wolf, Eva
通讯作者：
Wolf, Eva