SPECTROELECTROCHEMISTRY OF BLUE COPPER PROTEINS - PH AND TEMPERATURE DEPENDENCES OF THE REDUCTION POTENTIALS OF 5 AZURINS

被引：44

作者：

STCLAIR, CS ^{[1
]}

ELLIS, WR ^{[1
]}

GRAY, HB ^{[1
]}

机构：

[1] CALTECH,ARTHUR AMOS NOYES LAB,PASADENA,CA 91125

来源：

INORGANICA CHIMICA ACTA | 1992年 / 191卷 / 01期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/S0020-1693(00)80341-2

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

The pH and temperature dependences of the reduction potentials of Alcaligenes denitrificans (Ade), Pseudomonas aeruginosa (Pae), Alcaligenes faecalis (Afa), Alcaligenes sp. (Asp) and Bordetella bronchiseptica (Bbr) azurins have been determined by spectroelectrochemistry. Potentials at pH 8.0 (25-degrees-C, mu-0.1 M, NaP(i)) are: 267.0 (Ade); 291.9 (Pae); 251.5 (Afa); 278.1 (Asp); 250.3 (Bbr) mV versus NHE. The variations in the potentials with pH are interpreted in terms of interactions between the copper site and titrating histidine residues. Variations in the reduction potential of Bbr azurin with both pH and temperature indicate that the copper site is distorted significantly by a redox-linked conformational change in this protein.

引用

页码：149 / 155

页数：7

共 36 条

[1] CRYSTALLOGRAPHIC MODEL FOR AZURIN AT 3-A RESOLUTION [J].