Direct Measurements of the Cobalt-Thiolate Bonds Strength in Rubredoxin by Single-Molecule Force Spectroscopy.
| Autor: | Shi S; State Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, Jiangsu, 210023, China., Wu T; State Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, Jiangsu, 210023, China., Zheng P; State Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, Jiangsu, 210023, China. |
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| Jazyk: | angličtina |
| Zdroj: | Chembiochem : a European journal of chemical biology [Chembiochem] 2022 Jun 20; Vol. 23 (12), pp. e202200165. Date of Electronic Publication: 2022 May 11. |
| DOI: | 10.1002/cbic.202200165 |
| Abstrakt: | Cobalt is a trace transition metal. Although it is not abundant on earth, tens of cobalt-containing proteins exist in life. Moreover, the characteristic spectrum of Co(II) ion makes it a powerful probe for the characterization of metal-binding proteins through the formation of cobalt-ligand bonds. Since most of these natural and artificial cobalt-containing proteins are stable, we believe that these cobalt-ligand bonds in the protein system are also mechanically stable. To prove this, we used atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) to directly measure the rupture force of Co(II)-thiolate bond in Co-substituted rubredoxin (CoRD). By combining the chemical denature/renature method for building metalloprotein and cysteine coupling-based polyprotein construction strategy, we successfully prepared the polyprotein sample (CoRD) (© 2022 Wiley-VCH GmbH.) |
| Databáze: | MEDLINE |
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