Detecting transient protein-protein interactions by X-ray absorption spectroscopy:: The cytochrome c6-photosystem I complex

被引：7

作者：

Diaz-Moreno, Irene

Diaz-Quintana, Antonio

Subias, Gloria

Mairs, Trevor

De la Rosa, Miguel A.

Diaz-Moreno, Sofia

机构：

[1] Univ Seville, Inst Bioquim Vegetal & Fotosintesis, Seville 41092, Spain

[2] CSIC, Seville 41092, Spain

[3] Univ Zaragoza, Inst Ciencia Mat Aragon, E-50009 Zaragoza, Spain

[4] CSIC, Dept Fis Mat Condensada, E-50009 Zaragoza, Spain

[5] European Synchrotron Radiat Facil, F-38043 Grenoble, France

[6] Diamond Light Source Ltd, Rutherford Appleton Lab, Didcot OX1 0QX, Oxon, England

来源：

FEBS LETTERS | 2006年 / 580卷 / 13期

关键词：

cytochrome c(6); photosystem I; transient interactions; X-ray absorption spectroscopy;

D O I：

10.1016/j.febslet.2006.04.045

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：

Reliable analysis of the functionality of metalloproteins demands a highly accurate description of both the redox state and geometry of the metal centre, not only in the isolated metalloprotein but also in the transient complex with its target. Here, we demonstrate that the transient interaction between soluble cytochrome c(6) and membrane-embedded photosystem I involves subtle changes in the heme iron, as inferred by X-ray absorption spectroscopy (XAS). A slight shift to lower energies of the absorption edge of Fe2+ in cytochrome c(6) is observed upon interaction with photosystem I. This work constitutes a novel application of XAS to the analysis of weak complexes in solution. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：3023 / 3028

页数：6

共 26 条

[1] The structure and function of the cytochrome c2:: reaction center electron transfer complex from Rhodobacter sphaeroides [J].