Srajer V, Teng T, Ursby T, Pradervand C, Ren Z, Adachi S, Schildkamp W, Bourgeois D, Wulff M, Moffat K
Department of Biochemistry and Molecular Biology and the Consortium for Advanced Radiation Sources, University of Chicago, Chicago, IL 60637, USA.
Science. 1996 Dec 6;274(5293):1726-9. doi: 10.1126/science.274.5293.1726.
The biological activity of macromolecules is accompanied by rapid structural changes. The photosensitivity of the carbon monoxide complex of myoglobin was used at the European Synchrotron Radiation Facility to obtain pulsed, Laue x-ray diffraction data with nanosecond time resolution during the process of heme and protein relaxation after carbon monoxide photodissociation and during rebinding. These time-resolved experiments reveal the structures of myoglobin photoproducts, provide a structural foundation to spectroscopic results and molecular dynamics calculations, and demonstrate that time-resolved macromolecular crystallography can elucidate the structural bases of biochemical mechanisms on the nanosecond time scale.
大分子的生物活性伴随着快速的结构变化。在欧洲同步辐射装置中，利用肌红蛋白一氧化碳复合物的光敏性，在一氧化碳光解离后以及重新结合过程中，在血红素和蛋白质弛豫过程中获得具有纳秒时间分辨率的脉冲劳厄X射线衍射数据。这些时间分辨实验揭示了肌红蛋白光产物的结构，为光谱结果和分子动力学计算提供了结构基础，并证明时间分辨大分子晶体学能够在纳秒时间尺度上阐明生化机制的结构基础。
