Relationship between redox function and protein stability of cytochrornes c

被引：30

作者：

Terui, N

Tachiiri, N

Matsuo, H

Hasegawa, J

Uchiyama, S

Kobayashi, Y

Igarashi, Y

Sambongi, Y ^{[1
]}

Yamamoto, Y

机构：

[1] Hiroshima Univ, Grad Sch Biosphere Sci, Higashihiroshima 7398528, Japan

[2] Univ Tsukuba, Dept Chem, Tsukuba, Ibaraki 3058571, Japan

[3] Daiichi Pharmaceut Co Ltd, Edogawa Ku, Tokyo 1348630, Japan

[4] Osaka Univ, Grad Sch Engn, Suita, Osaka 5650871, Japan

[5] Osaka Univ, Grad Sch Pharmaceut Sci, Suita, Osaka 5650871, Japan

[6] Univ Tokyo, Dept Biotechnol, Tokyo 1138657, Japan

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2003年 / 125卷 / 45期

关键词：

D O I：

10.1021/ja035682f

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Electrochemical, 1H NMR, and optical studies on mesophile Pseudomonas aeruginosa cytochrome c551, its single (F34Y) and quintuple (F7A/V13M/F34Y/E43Y/V78I) mutants, and thermophile Hydrogenobacter thermophilus cytochrome c552 at wide temperature range demonstrated that the stable protein exhibits the low redox potential predominantly due to the enthalpic contribution to the redox reaction. The overall stability of the oxidized form was shown to determine the stability of the Fe-methionine coordination bond, which then directly regulates the redox function. Copyright © 2003 American Chemical Society.

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页码：13650 / 13651

页数：2

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