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铁硫蛋白的结构。

The structure of iron-sulfur proteins.

作者信息

Sticht H, Rösch P

机构信息

Lehrstuhl für Struktur und Chemie der Biopolymere, Universität Bayreuth, Germany.

出版信息

Prog Biophys Mol Biol. 1998;70(2):95-136. doi: 10.1016/s0079-6107(98)00027-3.

DOI:10.1016/s0079-6107(98)00027-3
PMID:9785959
Abstract

Ferredoxins are a group of iron-sulfur proteins for which a wealth of structural and mutational data have recently become available. Previously unknown structures of ferredoxins which are adapted to halophilic, acidophilic or hyperthermophilic environments and new cysteine patterns for cluster ligation and non-cysteine cluster ligation have been described. Site-directed mutagenesis experiments have given insight into factors that influence the geometry, stability, redox potential, electronic properties and electron-transfer reactivity of iron-sulfur clusters.

摘要

铁氧化还原蛋白是一类铁硫蛋白,最近已有大量关于它们的结构和突变数据。此前未知的适应嗜盐、嗜酸或嗜热环境的铁氧化还原蛋白结构以及用于簇连接和非半胱氨酸簇连接的新半胱氨酸模式已被描述。定点诱变实验使人们深入了解了影响铁硫簇的几何形状、稳定性、氧化还原电位、电子性质和电子转移反应性的因素。

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