title: The effects of biological environments on the electron-relay functionality of tryptophan residues in proteins.
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.
authors.affiliation: School of Chemistry and Chemical Engineering, Chongqing University, Chongqing 400030, China. chxh7@cqu.edu.cn
authors.forename: Xiaohua
authors.initials: X
authors.lastname: Chen
authors.forename: Hongjing
authors.initials: H
authors.lastname: Dai
authors.forename: Jilai
authors.initials: J
authors.lastname: Li
authors.forename: Xuri
authors.initials: X
authors.lastname: Huang
authors.forename: Zidong
authors.initials: Z
authors.lastname: Wei
mesh_terms: D004579:Electron Transport; D004583:Electrons; D058116:Lewis Acids / Q000737:chemistry; D008670:Metals / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D011789:Quantum Theory; D014364:Tryptophan / Q000737:chemistry*
chemical_list: D058116:Lewis Acids; D008670:Metals; D011506:Proteins; D014364:Tryptophan