Redox potential of azobenzene as an amino acid residue in peptides

被引：77

作者：

Boulegue, Cyril ^{[1
]}

Loeweneck, Markus ^{[1
]}

Renner, Christian ^{[1
]}

Moroder, Luis ^{[1
]}

机构：

[1] Max Planck Inst Biochem, D-82152 Martinsried, Germany

来源：

CHEMBIOCHEM | 2007年 / 8卷 / 06期

关键词：

azobenzenes; glutathione; peptides; redox chemistry; thermal isomerization; DNA-BINDING SPECIFICITY; CYCLIC-PEPTIDES; CONFORMATIONAL STATES; TRANS-AZOBENZENE; BETA-HAIRPIN; GLUTATHIONE; PHOTOMODULATION; SPECTROSCOPY; DISULFIDE; BACKBONE;

D O I：

10.1002/cbic.200600495

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：

Azobenzene is a common light switch. Azobenzene, as ω-amino acid derivative in peptides, exhibits redox properties that make it susceptible to reduction by thiols with concurrent thiol-induced enhanced thermal Z-to-E isomerization rates. (Chemical Equation Presented) © 2007 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：591 / 594

页数：4

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