Characterization of the pH-dependent resonance Raman transitions of archaeal and bacterial Rieske [2Fe-2S] proteins

被引：36

作者：

Iwasaki, T ^{[1
]}

Kounosu, A

Kolling, DRJ

Crofts, AR

Dikanov, SA

Jin, A

Imai, T

Urushiyama, A

机构：

[1] Nippon Med Coll, Dept Biochem & Mol Biol, Bunkyo Ku, Tokyo 1138602, Japan

[2] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA

[3] Univ Illinois, Dept Vet Clin Med, Urbana, IL 61801 USA

[4] Rikkyo St Pauls Univ, Dept Chem, Toshima Ku, Tokyo 1718501, Japan

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2004年 / 126卷 / 15期

关键词：

D O I：

10.1021/ja031976p

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The pH-dependent resonance Raman (RR) spectral changes of the cytochrome bc1-associated, high-potential Rieske proteins have frequently been invoked to explain the redox-linked ionization behavior. We report herein RR spectral data of archaeal and bacterial Rieske proteins that directly demonstrate the pH-dependent changes near and above pKa,ox2, but not around pKa,ox1, of the visible circular dichroism (CD) transitions. The RR spectral changes are attributed to modification of the immediate [2Fe-2S] cluster environment due to deprotonation of some exchangeable amide groups in the polypeptide backbone, rather than previously assumed simple changes of the Fe-Nimid stretching vibrations. Copyright © 2004 American Chemical Society.

引用

页码：4788 / 4789

页数：2

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