Electronic structure and its relation to function in copper proteins

被引：44

作者：

Szilagyi, RK ^{[1
]}

Solomon, EI ^{[1
]}

机构：

[1] Stanford Univ, Dept Chem, Stanford, CA 94305 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2002年 / 6卷 / 02期

基金：

美国国家科学基金会;

关键词：

D O I：

10.1016/S1367-5931(02)00304-6

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：

Spectroscopic and theoretical investigations of the geometric and electronic structures of mononuclear and binuclear copper sites in proteins help in understanding the contributions of these proteins to biological electron transfer. Spectroscopically calibrated density functional theory calculations, which give reasonable bonding descriptions in both ground and excited-states, define the role of the protein in determining the geometric and electronic structure of the active site.

引用

页码：250 / 258

页数：9

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