Instituto Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, 2780-157 Oeiras, Portugal.
iBET, Instituto de Biologia Experimental e Tecnológica, 2780-157 Oeiras, Portugal.
Molecules. 2022 Jun 23;27(13):4051. doi: 10.3390/molecules27134051.
Repair of Iron Center proteins (RIC) form a family of di-iron proteins that are widely spread in the microbial world. RICs contain a binuclear nonheme iron site in a four-helix bundle fold, two basic features of hemerythrin-like proteins. In this work, we review the data on microbial RICs including how their genes are regulated and contribute to the survival of pathogenic bacteria. We gathered the currently available biochemical, spectroscopic and structural data on RICs with a particular focus on RIC (also known as YtfE), which remains the best-studied protein with extensive biochemical characterization. Additionally, we present novel structural data for YtfE harboring a di-manganese site and the protein's affinity for this metal. The networking of protein interactions involving YtfE is also described and integrated into the proposed physiological role as an iron donor for reassembling of stress-damaged iron-sulfur centers.
铁中心蛋白(RIC)的修复形成了广泛存在于微生物世界中的二铁蛋白家族。RIC 包含位于四螺旋束折叠中的双核非血红素铁位点,这是血蓝蛋白样蛋白的两个基本特征。在这项工作中,我们回顾了有关微生物 RIC 的数据,包括它们的基因如何被调控以及如何有助于致病菌的存活。我们收集了目前可用的关于 RIC 的生化、光谱和结构数据,特别关注 RIC(也称为 YtfE),这是研究最广泛的蛋白,具有广泛的生化特性。此外,我们还提供了含有双锰位点的 YtfE 的新结构数据,以及该蛋白对这种金属的亲和力。还描述了涉及 YtfE 的蛋白质相互作用网络,并将其整合到作为应激损伤的铁-硫中心再组装的铁供体的生理作用中。