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

Authors

  • Dr. Xiaohua Chen,

    Corresponding author
    1. School of Chemistry and Chemical Engineering, Chongqing University, Chongqing 400030 (China)
    • School of Chemistry and Chemical Engineering, Chongqing University, Chongqing 400030 (China)
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  • Hongjing Dai,

    1. School of Chemistry and Chemical Engineering, Chongqing University, Chongqing 400030 (China)
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  • Dr. Jilai Li,

    1. State Key Laboratory of Theoretical and Computational Chemistry, Institute of Theoretical Chemistry, Jilin University, Changchun 130023 (China)
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  • Prof. Xuri Huang,

    Corresponding author
    1. State Key Laboratory of Theoretical and Computational Chemistry, Institute of Theoretical Chemistry, Jilin University, Changchun 130023 (China)
    • State Key Laboratory of Theoretical and Computational Chemistry, Institute of Theoretical Chemistry, Jilin University, Changchun 130023 (China)
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  • Prof. Zidong Wei

    1. School of Chemistry and Chemical Engineering, Chongqing University, Chongqing 400030 (China)
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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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