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Contribution of Time-Resolved Absorption Spectroscopy to Study Biological Questions

机译：时间分辨吸收光谱研究生物学问题的贡献

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In this report, we illustrate through the study of two allosteric heme proteins the contribution of time-resolved absorption spectroscopy to the under-standing of fundamental biological mechanisms. The first studied protein is the endogenous nitric oxide receptor (guanylate cyclase, sGC) whose activation and deactivation mechanisms are not yet fully resolved. We show that the rebinding of the proximal histidine occurs in ～100 picoseconds in sGC, which is the very first step of its deactivation following NO release. We also show that synergistic action of CO together with an allosteric activator induces the cleavage of the bond between heme iron and proximal histidine. The second one is the prototype of allosteric protein, the dioxygen transporter hemoglobin (Hb). In Hb, we show that the motion of the iron atom, central to the heme, moves in ～18 picoseconds after NO binding; this motion represents the very first step of the allosteric T → R transition.
机译：在本报告中，我们通过对两个颠覆血红素蛋白的研究说明了时间分辨吸收光谱对基本生物机制的局势的贡献。第一个研究的蛋白质是内源性一氧化氮受体（胍基环酶，SGC），其活化和失活机制尚未完全解决。我们表明，近端组氨酸的抗弯在SGC中发生在〜100皮秒内，这是其在没有释放后停用的第一步。我们还表明，CO的协同作用与颠振活化剂一起诱导血红素铁和近端组氨酸之间粘合的切割。第二个是颠覆蛋白质的原型，二恶英转运蛋白血红蛋白（HB）。在HB中，我们表明铁原子的运动，血红素的核心，在没有结合后在〜18粒秒中移动;该运动代表了颠覆性→R转变的第一步。

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