Ligand K-edge X-ray absorption spectroscopy: covalency of ligand-metal bonds

被引：324

作者：

Solomon, EI ^{[1
]}

Hedman, B

Hodgson, KO

Dey, A

Szilagyi, RK

机构：

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

[2] Stanford Synchrotron Radiat Lab, Stanford, CA 94309 USA

[3] Montana State Univ, Dept Chem & Biochem, Bozeman, MT 59717 USA

来源：

COORDINATION CHEMISTRY REVIEWS | 2005年 / 249卷 / 1-2期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

ligand K-edge XAS; Cu-A; blue copper; iron-sulfur cluster; nickel dithiolene; DFT;

D O I：

10.1016/j.ccr.2004.03.020

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

The ligand K-edge probes the ligand 1s --> valence np transitions. These transitions acquire intensity when the ligand is bound to an open shell metal ion. This intensity quantifies the amount of ligand character in the metal d orbitals, hence the covalency of the ligand-metal bond. In this review the methodology is developed and applied to copper proteins, iron-sulfur sites and nickel dithiolene complexes, as examples. These illustrate the power and impact of this method in evaluating covalency contributions to electron transfer pathways, reduction potentials, H-bond interactions, electron delocalization in mixed-valent systems and small molecule reactivity. (C) 2004 Elsevier B.V. All rights reserved.

引用

页码：97 / 129

页数：33

共 138 条

[1] THE STRUCTURE OF COPPER-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT 5 PH VALUES, WITH NO2- BOUND AND WITH TYPE-II COPPER DEPLETED [J].