Cupredoxins-A study of how proteins may evolve to use metals for bioenergetic processes

被引：66

作者：

Choi, Moonsung ^{[1
]}

Davidson, Victor L. ^{[1
]}

机构：

[1] Univ Mississippi, Med Ctr, Dept Biochem, Jackson, MS 39216 USA

来源：

METALLOMICS | 2011年 / 3卷 / 02期

关键词：

BLUE-COPPER PROTEINS; ELECTRON-TRANSFER REACTIONS; AROMATIC AMINE DEHYDROGENASE; CRYSTAL-STRUCTURE ANALYSIS; SITE-DIRECTED MUTAGENESIS; TRYPTOPHAN TRYPTOPHYLQUINONE ENZYME; PSEUDOMONAS-AERUGINOSA AZURIN; BOND MEDIATED RECOGNITION; CYTOCHROME C-551I COMPLEX; SELF-EXCHANGE RATES;

D O I：

10.1039/c0mt00061b

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：

Cupredoxins are small proteins that contain type I copper centers, which are ubiquitous in nature. They function as electron transfer shuttles between proteins. This review of the structure and properties of native cupredoxins, and those modified by site-directed mutagenesis, illustrates how these proteins may have evolved to specifically bind copper, develop recognition sites for specific redox partners, tune redox potential for a particular function, and allow for efficient electron transfer through the protein matrix. This is relevant to the general understanding of the roles of metals in energy metabolism, respiration and photosynthesis.

引用

页码：140 / 151

页数：12

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