Two- and four-pulse ESEEM studies of the heme binding center of a low-spin ferriheme protein: the importance of a multi-frequency approach

被引：42

作者：

Astashkin, AV ^{[1
]}

Raitsimring, AM ^{[1
]}

Walker, FA ^{[1
]}

机构：

[1] Univ Arizona, Dept Chem, Tucson, AZ 85721 USA

来源：

CHEMICAL PHYSICS LETTERS | 1999年 / 306卷 / 1-2期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

D O I：

10.1016/S0009-2614(99)00421-2

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The histamine complex of nitrophorin1 (NP1-Km) was studied by ESEEM at X- and S-bands. The proton sum combination feature in the X-band ESEEM spectra was well resolved at the low-field g-value(g(Z)), but unresolved at the high-field g-value (g(X)). Decreasing the microwave frequency down to S-band allowed us to obtain well-resolved ESEEM spectra at the g(X) position and to determine the orientation of g(X) to be 60 degrees-90 degrees with respect to the plane of the axial ligands. (C) 1999 Elsevier Science B.V. All rights reserved.

引用

页码：9 / 17

页数：9

共 20 条

[1] Nitric oxide binding and crystallization of recombinant nitrophorin I, a nitric oxide transport protein from the blood-sucking bug Rhodnius prolixus [J].