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首页> 外文期刊>Journal of Molecular Biology >Structural Basis of Novel Iron-Uptake Route and Reaction Intermediates in Ferritins from Gram-Negative Bacteria
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Structural Basis of Novel Iron-Uptake Route and Reaction Intermediates in Ferritins from Gram-Negative Bacteria

机译：革兰氏阴性细菌铁蛋白中新型铁吸收途径和反应中间体的结构基础

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摘要

Iron and oxygen chemistry is mediated by iron proteins for many biological functions. Carboxylate-bridged diiron enzymes including ferritin have the common mechanism of oxygen activation via peroxodiferric intermediates. However, the route for iron uptake and the structural identification of intermediates still remain incomplete. The 4-fold symmetry channel of Helicobacter pylori ferritin was previously proposed as the iron-uptake route in eubacteria, but the amino acid residues at the 4-fold channel are not highly conserved. Here, we show evidence for a short path for iron uptake from His93 on the surface to the ferroxidase center in H. pylori ferritin and Escherichia coli ferritin. The amino acid residues along this path are highly conserved in Gram-negative bacteria and some archaea, and the mutants containing S20A and H93L showed significantly decreased iron oxidation. Surprisingly, the E. coli ferritin S20A crystal structure showed oxygen binding and side-on, symmetric mu-eta(2):eta(2) peroxodiferric and oxodiferric intermediates. The results provide the structural basis for understanding the chemical nature of intermediates in iron oxidation in bacteria and some of archaea. (C) 2016 Elsevier Ltd. All rights reserved.
机译：铁和氧化学作用是由铁蛋白介导的，具有许多生物学功能。包括铁蛋白在内的羧酸桥联的二铁酶具有通过过二铁的中间体进行氧活化的常见机制。但是，铁的吸收途径和中间体的结构鉴定仍不完善。幽门螺杆菌铁蛋白的4倍对称通道以前被提议为真细​​菌中的铁摄取途径，但4倍通道上的氨基酸残基不是高度保守的。在这里，我们显示出从表面上的His93到幽门螺杆菌铁蛋白和大肠杆菌铁蛋白中的铁氧化物酶中心的铁吸收的短路径的证据。在革兰氏阴性细菌和一些古细菌中，沿着此路径的氨基酸残基高度保守，含有S20A和H93L的突变体显示铁的氧化显着降低。令人惊讶的是，大肠杆菌铁蛋白S20A晶体结构显示氧结合和侧，对称mu-eta（2）：eta（2）过二铁和氧二铁中间体。该结果为理解细菌和某些古细菌中铁氧化的中间体的化学性质提供了结构基础。 （C）2016 Elsevier Ltd.保留所有权利。

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