Spectroscopy and Electron Transfer Dynamics of Blue Copper Proteins

电子转移是生物化学中最关键的反应之一，而有效和可控的电子转移对生物来说是至关重要的。以铜为中心的金属蛋白在进行电子转移和了解蛋白质结构和功能之间的联系方面特别有效，这是许多生化和生物物理研究的核心。我们提出了一个研究计划，将新的理论发展(在诺丁汉和华威)与新的实验(在诺丁汉)交叉进行，以建立对蓝铜蛋白功能的详细理解，例如质蓝蛋白。在气相中生成活性中心的模型络合物，并测量它们的光谱。采用这种方法将允许直接研究活性中心的氧化和还原形式，并将提供关于配位配体的存在如何调节活性中心行为的信息。在此基础上，我们计划设计具有可调光谱特性的络合物。应用量子化学方法研究生物过程无疑是一个在不久的将来将迅速发展的研究领域。在量子力学/分子力学框架内，将对蛋白质的氧化和还原形式进行分子动力学模拟，并扩展到氧化形式的配体到金属的电荷转移状态。这些模拟将形成开发力场的基础，这些力场将用于研究电荷转移过程，并直接确定蛋白质的内在态的形式。

Electron transfer is one of the most crucial reactions in biochemistry and the efficient and controlled transfer of electrons is crucial to living organisms. Metalloproteins with copper centres are particularly effective at performing electron transfer and understanding the link between structure and function of proteins lies at the heart of much biochemical and biophysical research. We propose a programme of research that interleaves novel theoretical developments (at Nottingham and Warwick) with new experiments (at Nottingham) to build a detailed understanding of the function of blue copper proteins, such as plastocyanin. Model complexes of the active site will be generated in the gas-phase and their spectroscopy measured. Adopting this approach will allow the oxidised and reduced forms of the active site to be studied directly, and will furnish information on how the presence of the coordinating ligands modulates the behaviour of the active site. Building on this, we plan to design complexes with tunable spectroscopic properties. The application of quantum chemical methods to study biological processes is without doubt an area of research that will grow rapidly in the near future. Molecular dynamics simulations within a quantum mechanics/molecular mechanics framework will be performed for the oxidised and reduced forms of the protein, and extended to the ligand-to-metal charge transfer state of the oxidised form. These simulations will form the basis for the development of force fields that will be used to study the charge transfer process and establish the form of the entatic state of the protein directly.