Resonance Raman spectroscopy of Fe–S proteins and their redox properties

Resonance Raman spectroscopy of Fe–S proteins and their redox properties
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Fe-S 蛋白的共振拉曼光谱及其氧化还原性质

DOI:
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发表时间:
2018
期刊:
JBIC Journal of Biological Inorganic Chemistry
影响因子:
--
通讯作者:
M. Teixeira
M. Teixeira
中科院分区:
--
文献类型:
--
作者:
S. Todorović;M. Teixeira

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铁硫蛋白的共振拉曼光谱对簇的类型、结构和对称性敏感。此外,源自2Fe-2S、3Fe-4S和4Fe-4S簇中的桥接和末端Fe-S振动的带可以在光谱中灵敏地区分,以及非半胱氨酰配位配体的类型(如果存在的话)。因此,共振拉曼光谱技术在研究具有不同结构和功能的铁硫蛋白中发挥着非常积极的作用。我们在这里提供了可以从Fe-S簇的共振拉曼光谱获得的结构信息的简要概述,并且平行地,参考它们的热力学性质(例如,还原电位),它们共同定义了Fe-S蛋白的生理作用。我们展示了如何在过去几十年中获得的知识简单的集群,现在使复杂的结构,包括耦合到其他中心和瞬态过程,涉及集群相互转换,生物起源,拆卸和催化的Fe-S集群的研究。
Resonance Raman spectra of Fe–S proteins are sensitive to the cluster type, structure and symmetry. Furthermore, bands that originate from bridging and terminal Fe–S vibrations in the 2Fe–2S, 3Fe–4S and 4Fe–4S clusters can be sensitively distinguished in the spectra, as well as the type of non-cysteinyl coordinating ligands, if present. For these reasons, resonance Raman spectroscopy has been playing an exceptionally active role in the studies of Fe–S proteins of diverse structures and functions. We provide here a concise overview of the structural information that can be obtained from resonance Raman spectroscopy on Fe–S clusters, and in parallel, refer to their thermodynamic properties (e.g., reduction potential), which together define the physiological roles of Fe–S proteins. We demonstrate how the knowledge gained over the past several decades on simple clusters nowadays enables studies of complex structures that include Fe–S clusters coupled to other centers and transient processes that involve cluster inter-conversion, biogenesis, disassembly and catalysis.
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