Disentangling interfacial redox processes of proteins by SERR spectroscopy

被引：113

作者：

Murgida, Daniel H. ^{[1
]}

Hildebrandt, Peter ^{[2
]}

机构：

[1] Univ Buenos Aires, Dept Quim Inorgan, INQUIMAE, CONICET,Fac Ciencias Exactas & Nat, Buenos Aires, DF, Argentina

[2] Tech Univ Berlin, Inst Chem, D-10623 Berlin, Germany

来源：

CHEMICAL SOCIETY REVIEWS | 2008年 / 37卷 / 05期

关键词：

D O I：

10.1039/b705976k

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Surface-enhanced resonance-Raman spectroelectrochemistry represents a powerful approach for studying the structure and reaction dynamics of redox proteins immobilized on biocompatible electrodes in fundamental and applied sciences. Using this approach it has been recently shown that electric fields of biologically relevant magnitude are able to influence crucial parameters for the functioning of a variety of soluble and membrane bound heme proteins. Electric field effects discussed in this tutorial review include modulation of redox potentials, reorganization energies, protein dynamics and redox-linked structural changes.

引用

页码：937 / 945

页数：9

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