ArticleNature communications2015
Force-induced chemical reactions on the metal centre in a single metalloprotein molecule.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed.
- Bond breaking of furan-maleimide adductsChemical science · 2023Article
- An unexpected all-metal aromatic tetranuclear silver cluster in human copper chaperone Atox1.Chemical science · 2022Article
- Single-Molecule Force Spectroscopy Reveals Stability of mitoNEET and its [2Fe2Se] Cluster in Weakly Acidic and Basic Solutions.ChemistryOpen · 2022Article
- Review on the QM/MM Methodologies and Their Application to Metalloproteins.Molecules (Basel, Switzerland) · 2022Review
- Highly Dynamic Polynuclear Metal Cluster Revealed in a Single Metallothionein Molecule.Research (Washington, D.C.) · 2021Article
- Blue light-induced low mechanical stability of ruthenium-based coordination bonds: an AFM-based single-molecule force spectroscopy study.RSC advances · 2020Article
- Meeting report - NSF-sponsored workshop 'Progress and Prospects of Single-Molecule Force Spectroscopy in Biological and Chemical Sciences'.Journal of cell science · 2020Article
- The rupture mechanism of rubredoxin is more complex than previously thought.Chemical science · 2020Article
- Forcing the reversibility of a mechanochemical reaction.Nature communications · 2018Article
- Tailoring protein nanomechanics with chemical reactivity.Nature communications · 2017Article
- A highly stretchable autonomous self-healing elastomer.Nature chemistry · 2016Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Metalloproteins play indispensable roles in biology owing to the versatile chemical reactivity of metal centres. However, studying their reactivity in many metalloproteins is challenging, as protein three-dimensional structure encloses labile metal centres, thus limiting their access to reactants and impeding direct measurements. Here we demonstrate the use of single-molecule atomic force microscopy to induce partial unfolding to expose metal centres in metalloproteins to aqueous solution, thus allowing for studying their chemical reactivity in aqueous solution for the first time. As a proof-of-principle, we demonstrate two chemical reactions for the FeS4 centre in rubredoxin: electrophilic protonation and nucleophilic ligand substitution. Our results show that protonation and ligand substitution result in mechanical destabilization of the FeS4 centre. Quantum chemical calculations corroborated experimental results and revealed detailed reaction mechanisms. We anticipate that this novel approach will provide insights into chemical reactivity of metal centres in metalloproteins under biologically more relevant conditions.
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