Observation of sub-100 ps conformational changes in photolyzed carbonmonoxy-myoglobin probed by time-resolved circular dichroism
Observation of sub-100 ps conformational changes in photolyzed carbonmonoxy-myoglobin probed by time-resolved circular dichroism
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DOI：
10.1016/j.cplett.2005.09.022
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发表时间：
2005-11-11
影响因子：
2.8
通讯作者：
Hache, F
中科院分区：
文献类型：
--
作者：
Dartigalongue, T;Hache, F
对碳单氧肌红蛋白进行了时间分辨圆二色性 (CD) 实验。配体解离后以亚皮秒时间分辨率测量 CD，并通过基于极化理论的经典 CD 计算来解释数据。我们观察到 CD 信号在几皮秒内减少，并且向稳态脱氧肌红蛋白值松弛了 100 ps 以下，我们将其归因于近端组氨酸的应力，随着蛋白质从配体几何结构到去配体几何结构的整体重组而松弛。 (c) 2005 Elsevier B.V. 保留所有权利。
A time-resolved circular dichroism (CD) experiment is carried out on carbonmonoxy-myoglobin. The CD is measured with a sub-picosecond time resolution after ligand dissociation and the data are interpreted thanks to a classical CD calculation based on the polarizability theory. We observe a decrease of the CD signal in a few picoseconds and a sub-100 ps relaxation towards steady-state deoxy-myoglobin values which we assign to a stress of the proximal histidine which relaxes with the global reorganization of the protein from its liganded geometry to its deliganded one. (c) 2005 Elsevier B.V. All rights reserved.