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The Effects of Biological Environments on the Electron‐Relay Functionality of Tryptophan Residues in Proteins
Author(s) -
Chen Xiaohua,
Dai Hongjing,
Li Jilai,
Huang Xuri,
Wei Zidong
Publication year - 2012
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201100713
Subject(s) - chemistry , tryptophan , electron transfer , intermolecular force , electron transport chain , lewis acids and bases , electron affinity (data page) , protein structure , photochemistry , biophysics , molecule , biochemistry , amino acid , organic chemistry , biology , catalysis
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.