细菌视紫红质（Bacteriorhodopsin's sense of light）的光电流机制
On the mechanisms responsible of photocurrent in bacteriorhodopsin (Bacteriorhodopsin's sense of light)
摘要：
近年来，细菌视紫红质（bR），一种跨膜蛋白家族的蛋白质，其电学性质受到越来越多的关注。考虑到电流的结构依赖性，在之前的一组论文中，我们提出了相邻氨基酸之间的顺序隧穿机制。事实上，人们普遍认为，当用绿光照射时，bR在分子水平上发生构象变化。因此，蛋白质三级结构在模拟电荷转移中所起的作用不可忽视。本文的目的是超越以前的模型，在一个新的电子学分支的框架内，我们称之为蛋白电子学，它利用蛋白质作为可靠的，众所周知的材料的能力，用于开发新型生物电子器件。特别地，本方法假设构象变化不是蛋白质在光照射时经历的唯一转化。相反，光还可以促进蛋白质状态的自由能增加，这反过来又会改变其内部连接度，这里用与氨基酸之间物理相互作用相关的相互作用半径值的变化来描述。实现的模型，使我们能够实现更好的协议在该地区的低应用偏差的理论和实验之间的协议，通过保持在高值的应用偏差的协议水平。此外，研究结果提供了新的见解负责bR光响应的机制。
英文摘要：
Recently, a growing interest has been addressed to the electrical properties of bacteriorhodopsin (bR), a protein belonging to the transmembrane protein family. To take into account the structure-dependent nature of the current, in a previous set of papers we suggested a mechanism of sequential tunneling among neighbouring amino acids. As a matter of fact, it is well accepted that, when irradiated with green light, bR undergoes a conformational change at a molecular level. Thus, the role played by the protein tertiary-structure in modeling the charge transfer cannot be neglected. The aim of this paper is to go beyond previous models, in the framework of a new branch of electronics, we called proteotronics, which exploits the ability to use proteins as reliable, well understood materials, for the development of novel bioelectronic devices. In particular, the present approach assumes that the conformational change is not the unique transformation that the protein undergoes when irradiated by light. Instead, the light can also promote a free-energy increase of the protein state that, in turn, should modify its internal degree of connectivity, here described by the change in the value of an interaction radius associated with the physical interactions among amino acids. The implemented model enables us to achieve a better agreement between theory and experiments in the region of a low applied bias by preserving the level of agreement at high values of applied bias. Furthermore, results provide new insights on the mechanisms responsible for bR photoresponse.
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