ArticleBiophysical journal2011
Direct measurements of the mechanical stability of zinc-thiolate bonds in rubredoxin by single-molecule atomic force microscopy.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 30 citations in OpenAlex.
- Azobenzene as a photoswitchable mechanophore.Nature chemistry · 2024Article
- An unexpected all-metal aromatic tetranuclear silver cluster in human copper chaperone Atox1.Chemical science · 2022Article
- Protein folding mechanism revealed by single-molecule force spectroscopy experiments.Biophysics reports · 2021Article
- Targeting a Dark Excited State of HIV-1 Nucleocapsid by Antiretroviral Thioesters Revealed by NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2018Article
- Multidomain proteins under force.Nanotechnology · 2017Article
- The mechanochemistry of copper reports on the directionality of unfolding in model cupredoxin proteins.Nature communications · 2015Article
- Single-molecule dynamics and mechanisms of metalloregulators and metallochaperones.Biochemistry · 2013Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
Zinc (Zn) is one of the most abundant metals and is essential for life. Through ligand interactions, often with thiolate from cysteine residues in proteins, Zn can play important structural roles in organizing protein structure and augmenting protein folding and stability. However, it is difficult to separate the contributions of Zn-ligand interactions from those originating from intrinsic protein folding in experimental studies of Zn-containing metalloproteins, which makes the study of Zn-ligand interactions in proteins challenging. Here, we used single-molecule force spectroscopy to directly measure the mechanical rupture force of the Zn-thiolate bond in Zn-rubredoxin. Our results show that considerable force is needed to rupture Zn-thiolate bonds (~170 pN, which is significantly higher than the force necessary to rupture the coordination bond between Zn and histidines). To our knowledge, our study not only provides new information about Zn-thiolate bonds in rubredoxin, it also opens a new avenue for studying metal-ligand bonds in proteins using single-molecule force spectroscopy.
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