...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Methionine Ligand Lability in Bacterial Monoheme Cytochromes c: An Electrochemical Study
【24h】

Methionine Ligand Lability in Bacterial Monoheme Cytochromes c: An Electrochemical Study

机译：细菌单血红素细胞色素中蛋氨酸的配体不稳定性c：一项电化学研究

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The direct electrochemical analysis of adsorbed redox active proteins has proven to be a powerful technique in biophysical chemistry, frequently making use of the electrode material pyrolytic "edge-plane" graphite. However, many heme-bearing proteins such as cytochromes c have been also examined systematically at alkanethiol-modified gold surfaces, and previously we reported the characterization of the redox properties of a series of bacterial cytochromes c in a side-by-side comparison of carbon and gold electrode materials. In our prior findings, we reported an unanticipated, low potential (E_m ~ —100 mV vs SHE) redox couple that could be analogously observed when a variety of monoheme cytochromes care adsorbed onto carbon-based electrodes. Here we demonstrate that our prior phenomological data can be understood quantitatively in the loss of the methionine ligand of the heme iron, using the cytochrome c from Hydrogenbacter thermophilum as a model system. Through the comparison of wild-type protein with M61H and M61A mutants, in direct electrochemical analyses conducted as a function of temperature and exogenous ligand concentration, we are able to show that Met-ligated cytochromes c have a propensity to lose their Met ligand at graphite surfaces, and that energetics of this process (63 ± 0.2kJ/mol) is similar to the energies associated with "foldons" of known protein folding pathways.
机译：吸附的氧化还原活性蛋白的直接电化学分析已被证明是生物物理化学中的一项强大技术，经常使用电极材料热解“边缘平面”石墨。但是，许多含血红素的蛋白质（例如细胞色素c）也已在链烷硫醇修饰的金表面上进行了系统检查，并且先前我们报道了一系列细菌细胞色素c的碳的并列比较的表征。和金电极材料。在我们先前的发现中，我们报告了一个意想不到的低电位（E_m〜-100 mV vs SHE）氧化还原电对，当多种单血红素细胞色素被吸附到碳基电极上时，可以类似地观察到。在这里，我们证明了使用嗜热氢细菌的细胞色素c作为模型系统，可以定量了解血红素铁的蛋氨酸配体的损失，从而了解我们先前的物候数据。通过将野生型蛋白与M61H和M61A突变体进行比较，在根据温度和外源配体浓度进行的直接电化学分析中，我们能够证明Met连接的细胞色素c有失去其Met配体的倾向表面，并且此过程的能量（63±0.2kJ / mol）类似于与已知蛋白质折叠途径的“折叠”相关的能量。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号