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The Effects of Biological Environments on the Electron-Relay Functionality of Tryptophan Residues in Proteins

✍ Scribed by Dr. Xiaohua Chen; Hongjing Dai; Dr. Jilai Li; Prof. Xuri Huang; Prof. Zidong Wei

Publisher
John Wiley and Sons
Year
2011
Tongue
English
Weight
851 KB
Volume
13
Category
Article
ISSN
1439-4235

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✦ Synopsis

Abstract

Clarifying the contribution of tryptophan (Trp) to electron‐transfer (ET) processes in different protein surroundings can help to understand the effective pathway of ET in proteins. Interactions between Trp residues and protein microsurroundings involve intermolecular H‐bonds, cation and π‐electron clouds of aromatic rings, the secondary structure and π orbital of aromatic rings, and so on. Detailed analyses reveal that the microsurroundings play an important role in modulating the electron‐relay function of Trp in proteins. Generally, microsurroundings with strong Lewis acidity inhibit electron hole transport through Trp residues. Systems with weak Lewis acidity finely tune the electron‐relay ability of Trp in proteins, while those with strong Lewis basicity strongly enhance the electron‐relay ability of Trp residues.

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