The structure of iron-sulfur proteins

被引：117

作者：

Sticht, H ^{[1
]}

Rösch, P ^{[1
]}

机构：

[1] Univ Bayreuth, Lehrstuhl Struktur & Chem Biopolymere, D-95447 Bayreuth, Germany

来源：

PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY | 1998年 / 70卷 / 02期

关键词：

iron-sulfur proteins; ferredoxins; HiPIPs; structure; mutational studies; stability;

D O I：

10.1016/S0079-6107(98)00027-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 1998 Elsevier Science Ltd. All rights reserved.

引用

页码：95 / 136

页数：42

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