Investigation of the redox-dependent modulation of structure and dynamics in human cytochrome c
Investigation of the redox-dependent modulation of structure and dynamics in human cytochrome c
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DOI：
10.1016/j.bbrc.2015.12.079
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发表时间：
2016-01-22
影响因子：
3.1
通讯作者：
Ishimori, Koichiro
中科院分区：
文献类型：
--
作者：
Imai, Mizue;Saio, Tomohide;Ishimori, Koichiro
用溶液核磁共振研究了人细胞色素c（Cyt c）的结构和动力学的氧化还原依赖性变化。我们发现在几个区域，包括残基23-28（环3），这是进一步证实了还原和氧化状态的细胞色素c之间的化学位移差异显着的结构变化。这些差异是必不可少的歧视细胞色素c氧化酶（CcO）在电子转移反应过程中的氧化还原状态。Carr-Purcell-Meiboom-Gill（CPMG）弛豫分散实验发现，His 33周围的区域在μ s-ms时间尺度上经历构象交换，表明显著的氧化还原依赖性结构变化。由于His 33不是CcO相互作用位点的一部分，我们的数据表明，该区域的动态特性，这是远离CcO的相互作用位点，有助于电子转移到CcO过程中的构象变化。(C)2015 Elsevier Inc. All rights reserved.
Redox-dependent changes in the structure and dynamics of human cytochrome c (Cyt c) were investigated by solution NMR. We found significant structural changes in several regions, including residues 23-28 (loop 3), which were further corroborated by chemical shift differences between the reduced and oxidized states of Cyt c. These differences are essential for discriminating redox states in Cyt c by cytochrome c oxidase (CcO) during electron transfer reactions. Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion experiments identified that the region around His33 undergoes conformational exchanges on the mu s-ms timescale, indicating significant redox-dependent structural changes. Because His33 is not part of the interaction site for CcO, our data suggest that the dynamic properties of the region, which is far from the interaction site for CcO, contribute to conformational changes during electron transfer to CcO. (C) 2015 Elsevier Inc. All rights reserved.