Investigating the structure and function of cupredoxins

被引：139

作者：

Dennison, C ^{[1
]}

机构：

[1] Univ Newcastle Upon Tyne, Sch Med, Inst Cell & Mol Biosci, Newcastle Upon Tyne NE2 4HH, Tyne & Wear, England

来源：

COORDINATION CHEMISTRY REVIEWS | 2005年 / 249卷 / 24期

基金：

英国生物技术与生命科学研究理事会;

关键词：

metalloproteins; copper proteins; cupredoxins; phytocyanins; electron transfer; mutagenesis;

D O I：

10.1016/j.ccr.2005.04.021

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

Copper is widely used in nature to promote electron transfer in a variety of processes. The metal is usually found as a mononuclear type I copper site protected by a protein envelope, which has become known as a cupredoxin fold. In the past few years, the use of protein engineering combined with various spectroscopic and kinetic approaches has provided detailed information about cupredoxins and cupredoxin domains. This review will describe some of the recent advances that have been made, highlighting that there is still a long way to go before we fully appreciate the complexity of biological electron transfer proteins. (c) 2005 Elsevier B.V. All rights reserved.

引用

页码：3025 / 3054

页数：30

共 342 条

[1] The structure of Acidithiobacillus ferrooxidans c4-cytochrome:: A model for complex-induced electron transfer tuning [J].