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Photoactivation of the cryptochrome/photolyase superfamily

机译:隐色素/光解酶超家族的光活化

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The cryptochrome/photolyase superfamily is a class of flavoproteins that can regulate the growth and development in plants, as well as the circadian clock and the potential magnetic navigation in animals, primarily by absorbing UV-A and blue light. It is generally agreed that these functions depend on the photochemical reaction of the flavin adenine dinucleotide (FAD) chromophore, non-covalently binding to cryptochromes or photolyases. Irradiation can initiate either photoreduction between FAD and certain electron donors or electron jumping in FAD, thereby leading to the generation of intermediates that activate the protein. This signaling process is known as photoactivation. Subsequently, the activated protein will interact with downstream receptors to transfer the photo and magnetic signals. Based on in-depth research on photoactivation, two photo-cycle mechanisms for the photoreception/photosignaling of the cryptochrome/photolyase superfamily, i.e., the photolyase model and the phototropin model, have been proposed. There is no apparent alternative to the photo-cycle of cyclobutane pyrimidine dimer (CPD) or (6-4) photolyase following the photolyase model. However, the mechanism is not clear for the photoactivation of ayptochromes and CRY-DASH, a new subcategory of photolyase. Since the photoactivation process is the first step for the physiological function of proteins, more and improved research efforts in this field have been widely developed. This review first briefly presents the structure, the photoactivation, and the repair mechanism of CPD and (6-4) photolyase. Next, we review in detail the photoactivation of cryptochromes and CRY-DASH by analyzing the current status of research, as well as the contradictions in the resting redox states of FAD, intermediates in photoreactions, the photo-cycle of FAD, the signaling state of proteins, and the necessity of given tryptophans for protein activity. Based on these studies, the correlations of photoactivation and photo-cycle mechanisms, as well as the correlations of photoactivation and magnetoreception of proteins, are discussed. Finally the crucial open questions regarding the photoactivation mechanisms of the cryptochrome/photolyase superfamily are outlined, considering the hypothesis for a cryptochrome-based model of avian magnetoreception. (C) 2014 Elsevier B.V. All rights reserved.
机译:隐花色素/光裂解酶超家族是一类黄素蛋白,主要通过吸收UV-A和蓝光来调节植物,生物钟和动物体内潜在的磁导航的生长和发育。通常认为,这些功能取决于黄素腺嘌呤二核苷酸(FAD)发色团的光化学反应,它们非共价结合至隐色染料或光裂解酶。辐射可以引发FAD和某些电子供体之间的光还原,也可以引发FAD中的电子跳跃,从而导致激活蛋白质的中间体的产生。这种信号传导过程称为光激活。随后,活化的蛋白质将与下游受体相互作用以转移光和磁信号。基于对光激活的深入研究,提出了两种用于隐色染料/光裂解酶超家族的光接收/光信号传递的光循环机制,即光裂解酶模型和光养蛋白模型。遵循光裂解酶模型,环丁烷嘧啶二聚体(CPD)或(6-4)光裂解酶的光循环没有明显的替代选择。但是,尚不清楚该机制对aytotochromes和CRY-DASH(一种新的光裂解酶亚类)的光活化作用。由于光活化过程是蛋白质生理功能的第一步,因此,在该领域中已进行了越来越多的改进研究工作。本文首先简要介绍了CPD和(6-4)光裂解酶的结构,光活化和修复机理。接下来,我们通过分析研究现状,FAD的静态氧化还原状态,光反应中间体,FAD的光循环,FAD的信号状态等方面的矛盾,来详细回顾隐色染料和CRY-DASH的光活化。蛋白质,以及给定色氨酸进行蛋白质活性的必要性。基于这些研究,讨论了光激活和光循环机制的相关性,以及蛋白质的光激活和磁感受性的相关性。最后,考虑到基于隐色染料的禽磁感受模型的假设,概述了有关隐色染料/光合酶超家族的光激活机制的关键开放性问题。 (C)2014 Elsevier B.V.保留所有权利。

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