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Understanding the NO-Sensing Mechanism at Molecular Level

机译：理解分子水平的无感应机制

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We present here how ultrafast time-resolved spectroscopy improves our understandingof a new class of proteins: Nitric Oxide sensors. Nitric oxide (NO) is a small, short-lived, andhighly reactive gaseous molecule and it acts as a second messenger in several physiological sys-tems. NO sensors are proteins which bind NO and are able to translate this binding into a signalfor mammal cells as well as in bacteria. We have studied NO-sensors with the goal of understand-ing the activation and deactivation mechanism of the human NO-receptor, the enzyme guanylatecyclase (sGC), which is involved in communication between cells. Some bacterial sensors of NO(SONO) have structural homologies and common properties with sGC, but also have differenceswith sGC which make them valuable system to get structural and physiological information onsGC. To understand how NO-sensors interact with NO and control its reactivity, it is essential toprobe dynamics and interactions when NO is present within protein core and what are the associ-ated structural changes. For this purpose, we have used time-resolved absorption spectroscopy inthe picoseconds (10~(-12)s) time domain. NO can be photodissociated from heme by the pulse of fem-tosecond laser. Time-resolved transient absorption spectra on NO-sensors were recorded andNO-protein interacttion were recorded. In case of cytochrome c', we identified the formation of5-coordinate (5c)-NO and 5c-His hemes from 4c-heme and demonstrate that proximal histidineprecludes NO rebinding at the proximal site. In bacteria, the adaptation of SONO to temperaturechanges was not achieved by a simple temperature-dependent NO binding equilibrium, but by achange of the proportion between 5c-NO and 6c-NO species. This amplifies the response to tem-perature changes since a fast NO rebinding is the only property of a 5c-NO leading to 4c-heme af-ter dissociation. Our results of NO dynamics provide a model for the regulation at molecular levelin NO-sensing function.
机译：我们在这里介绍超快时间分辨的光谱学改善我们对新类蛋白质的理解：一氧化氮传感器。一氧化氮（NO）是小，短寿命，高反应性的气态分子，并且其用作几种生理系统中的第二信使。没有传感器是蛋白质，其粘合否并能够将该结合转化为哺乳动物细胞以及细菌中的信号。我们已经研究了No-VERSORS，目的是了解人类无受体的激活和失活机制，酶胍基琥珀酰基（SGC），其参与细胞之间的沟通。一些NO（SONO）的细菌传感器具有结构性同源物和具有SGC的常见性质，但也具有SGC的差异，使其使其有价值的系统来获得结构和生理信息。为了了解NO - 传感器如何与NO和控制其反应性，当NO在蛋白质核心存在时，它是必要的拓趾动态和相互作用，并且有关的结构变化是什么。为此目的，我们使用了时间分辨的吸收光谱InthePic秒（10〜（-12）时的时域。不能通过FEM-TOSECOND激光的脉冲从血红素光调。记录了NO传感器上的时间分离的瞬态吸收光谱。记录了ANDNO-蛋白质互动。在细胞色素C'的情况下，我们鉴定了来自4℃-血红素的5-坐标（5C）-NO和5C-他的血液的形成，并证明了近端部位的近端部位没有重新剥离。在细菌中，通过简单的温度依赖性的无结合平衡来实现Sono到温度的适应，但通过5C-NO和6C-NO物种之间的比例的achange。这可以放大对TEM-CHERITITE变化的响应，因为快速的叛乱是5C-NO导致4C-HEME AF-TER解离的唯一属性。我们的No Dynamics的结果为分子水平无传感功能的调节提供了一种模型。

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