Direct Measurements of the Cobalt-Thiolate Bonds Strength in Rubredoxin by Single-Molecule Force Spectroscopy.
biophysics
cobalt-thiolate bonds
metalloproteins
rubredoxin
single molecule-force spectroscopy
Journal
Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360
Informations de publication
Date de publication:
20 06 2022
20 06 2022
Historique:
revised:
26
04
2022
received:
24
03
2022
pubmed:
28
4
2022
medline:
23
6
2022
entrez:
27
4
2022
Statut:
ppublish
Résumé
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)
Identifiants
pubmed: 35475313
doi: 10.1002/cbic.202200165
doi:
Substances chimiques
Ligands
0
Metalloproteins
0
Metals
0
Polyproteins
0
Rubredoxins
0
Cobalt
3G0H8C9362
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e202200165Informations de copyright
© 2022 Wiley-VCH GmbH.
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