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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR
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Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR

机译：顺磁性NMR测定细胞色素c和细胞色素c过氧化物酶复合物的溶液结构和动力学

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摘要

The physiological complex of yeast cytochrome c peroxidase and iso-1-cytochrome c is a paradigm for biological electron transfer. Using paramagnetic NMR spectroscopy, we have determined the conformation of the protein complex in solution, which is shown to be very similar to that observed in the crystal structure [Pelletier H, Kraut J (1992) Science 258:1748-1755]. Our results support the view that this transient electron transfer complex is dynamic. The solution structure represents the dominant protein-protein orientation, which, according to our estimates, is occupied for > 70% of the lifetime of the complex, with the rest of the time spent in the dynamic encounter state. Based on the observed paramagnetic effects, we have delineated the conformational space sampled by the protein molecules during the dynamic part of the interaction, providing experimental support for the theoretical predictions of the classical Brownian dynamics study [Northrup SH, Boles JO, Reynolds JCL (1988) Science 241:67-70]. Our findings corroborate the dynamic behavior of this complex and offer an insight into the mechanism of the protein complex formation in solution.
机译：酵母细胞色素c过氧化物酶和异-1-细胞色素c的生理复合物是生物电子转移的范例。使用顺磁性NMR光谱法，我们已经确定了溶液中蛋白质复合物的构象，这显示出与在晶体结构中观察到的构象非常相似[Pelletier H，Kraut J（1992）Science 258：1748-1755]。我们的结果支持了这种瞬态电子转移络合物是动态的观点。溶液的结构代表了主要的蛋白质-蛋白质方向，根据我们的估计，该复合物在复合物寿命中占> 70％，其余时间则处于动态相遇状态。基于观察到的顺磁效应，我们划定了相互作用过程中蛋白质分子在相互作用的动态部分采样的构象空间，为经典布朗动力学研究的理论预测提供了实验支持[Northrup SH，Boles JO，Reynolds JCL（1988 （《科学》 241：67-70）。我们的发现证实了该复合物的动态行为，并提供了对溶液中蛋白质复合物形成机理的深入了解。

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