Iron-sulfur cluster electronic structural evolution and its contribution to diverse functionality

铁硫簇电子结构演化及其对多种功能的贡献

• 批准号: 310983376
• 负责人: Professorin Dr. Serena DeBeer
• 金额: --
• 依托单位: Max-Planck-Institut für Kohlenforschung
• 依托单位国家: 德国
• 项目类别: Priority Programmes
• 财政年份: 2016
• 资助国家: 德国
• 起止时间: 2015-12-31 至 2022-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/310983376?language=en
• 关键词: Iron; sulfur; cluster; electronic; structural

This proposal builds upon the results that the applicants have obtained in the first funding period of the SPP 1927 and that have already led to five publications from our own groups and in collaboration with other SPP members. The project is centered around understanding the detailed electronic structure of complex iron-sulfur clusters in nature and in model systems. The ultimate goal is to develop insight into the unique reactivity of these systems, with special emphasis on nitrogenase and hydrogenase. The first funding period contained a spectroscopy- and a theory-oriented branch of research. In the spectroscopy-oriented part, 2p3d resonant inelastic x-ray scattering (RIXS) and X-ray magnetic circular dichroism (XMCD) have been developed as unique probes of the local electronic structure of Fe/S sites. The theoretical research was directed towards developing new model Hamiltonians on the basis of detailed first-principle wavefunction based calculations that will allow the calculation of spectroscopic observables for oligonuclear clusters, which are too complex to be rigorously treated by quantum chemistry. In the present proposal, both branches of research will be further extended and are expected to eventually converge into unique combined experimental and theoretical protocol for the elucidation of Fe/S site electronic structure. To this end, our 2p3d RIXS studies will focus on obtaining higher resolution data to further enhance the quantitative information. In addition, we will further explore XMCD as a complementary, powerful technique for the study of Fe/S sites and will apply it to the active sites of nitrogenase, as well hydrogenase. In parallel with the experimental developments, we will continue our studies on ab initio derived model Hamiltonians. Presently, these studies cover monomeric and dimeric Fe/S sites in detail. The major goal of the second funding period is to develop the necessary framework to treat higher nuclearities from trimers and tetramers, all the way to the FeMoco active sites of nitrogenase, the most complex active site in biology. We will also put major emphasis on developing the necessary framework to calculate magnetic and X-ray spectroscopic properties from the model Hamiltonian treatment. Eventually, we hope to utilize the developed protocols to obtain fundamental insights into the electronic structural consequences of nature’s evolved biosynthetic pathways in FeS cluster assembly. In addition to exploring these new research areas, we will continue and intensify our collaborative efforts in the SPP with the groups of Franc Meyer, Oliver Einsle and Matthias Boll, among others.

该提案建立在申请人在 SPP 1927 第一个资助期间获得的成果的基础上，这些成果已经导致我们自己的小组与其他 SPP 成员合作发表了五篇出版物。该项目的重点是了解详细的电子结构。最终目标是深入了解这些系统的独特反应性，特别强调固氮酶和氢化酶。的在光谱学方面，开发了2p3d共振非弹性X射线散射（RIXS）和X射线磁圆二色性（XMCD）作为Fe/S位点局域电子结构的独特探针进行理论研究。在详细的第一原理波函数计算的基础上，指导开发新模型哈密顿量，这将允许计算寡核团簇的光谱可观测值，因为寡核团簇过于复杂而难以计算。在目前的提案中，这两个研究分支将得到进一步扩展，并有望最终汇聚成独特的组合实验和理论方案，以阐明 Fe/S 位点电子结构。研究将侧重于获得更高分辨率的数据，以进一步增强定量信息。此外，我们将进一步探索 XMCD 作为研究 Fe/S 位点的补充、强大技术，并将其应用于固氮酶的活性位点。氢化酶。在实验进展的同时，我们将继续对从头算起的哈密顿量模型进行研究。目前，这些研究详细涵盖了单体和二聚体 Fe/S 位点。第二期资助的主要目标是开发必要的框架来治疗。从三聚体和四聚体到固氮酶的 FeMoco 活性位点（生物学中最复杂的活性位点），我们还将重点开发必要的框架，以根据哈密顿量模型计算磁和 X 射线光谱特性。最终，我们希望利用已开发的方案来获得对 FeS 簇组装中自然进化生物合成途径的电子结构后果的基本了解。除了探索这些新的研究领域外，我们还将继续并加强我们在 SPP 方面的合作。与 Franc Meyer、Oliver Einsle 和 Matthias Boll 等团体合作。