Chemistry Letters
Online ISSN : 1348-0715
Print ISSN : 0366-7022
ISSN-L : 0366-7022
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Vol. 50 Commemorative Highlight Review
  • Jingyuan Nie, Fang Tian, Bin Zheng, Ziyi Wang, Peng Zheng
    2021 Volume 50 Issue 9 Pages 1667-1675
    Published: September 05, 2021
    Released: September 15, 2021

    Thanks to the binding of various metal ions, metalloprotein plays an essential role in many different biological processes and represents an indispensable protein subgroup. Thus, the knowledge of the incorporated metal site and metal-ligand coordination bond in the protein is invaluable for understanding this critical bio-macromolecule and designing a new one. Over the last decade, atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) has been used to explore the metalloprotein as an emerging methodology, focusing on measuring metal-ligand bond strength. By stretching the protein molecule along its peptide backbone, AFM-SMFS can unfold the protein secondary structure and break and quantify the metal-ligand bond/metal cluster. Moreover, the very recent development of enzymatic, site-specific protein conjugation and immobilization methods for the SMFS system enables the highly efficient and accurate measurement of the metal-ligand bond strength in proteins. As a result, comparing the strength among different types of metal-ligand bonds in proteins becomes possible, and the trend of their strength is gradually revealed, such as the Fe(III)-ligand bond in iron-binding proteins. Thus, we envision that in the future AFM-SMFS may provide a unique insight to uncover the general principle of how protein selectively binds to metal ion.

    Metalloprotein plays an essential role in many biological processes, thanks to the incorporation of metal sites/metal-ligand bonds. Over the last decade, atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) has been used to explore the metalloprotein, focusing on the measurment of metal-ligand bond strength. Assited with the enzymatic protein immoblization methods, the strength of Fe(III)-ligand bonds in proteins have been accurately measured, revealing their trend as Fe-S∼Fe-O >> Fe-N. Fullsize Image