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

摘要

Clarifying the contribution of tryptophan (Trp) to electrontransfer (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,microsur roundings with strong Lewis acidity inhibit electron hole trans port 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.