ArticleBiomolecules2019
Tuning Structure and Dynamics of Blue Copper Azurin Junctions via Single Amino-Acid Mutations.
Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Efficient Electron Hopping Transport through Azurin-Based Junctions.The journal of physical chemistry letters · 2023Article
- Copper coordination states affect the flexibility of copper Metallochaperone Atox1: Insights from molecular dynamics simulations.Protein science : a publication of the Protein Society · 2022Article
- Artificial Photosynthesis: Is Computation Ready for the Challenge Ahead?Nanomaterials (Basel, Switzerland) · 2021Review
- Protein Binding and Orientation Matter: Bias-Induced Conductance Switching in a Mutated Azurin Junction.Journal of the American Chemical Society · 2020Article
- Multifaceted aspects of charge transfer.Physical chemistry chemical physics : PCCP · 2020Article
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Authors and funding
6 authors.
Funding
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Abstract
In the growing field of biomolecular electronics, blue-copper Azurin stands out as one of the most widely studied protein in single-molecule contacts. Interestingly, despite the paramount importance of the structure/dynamics of molecular contacts in their transport properties, these factors remain largely unexplored from the theoretical point of view in the context of single Azurin junctions. Here we address this issue using all-atom Molecular Dynamics (MD) of Pseudomonas Aeruginosa Azurin adsorbed to a Au(111) substrate. In particular, we focus on the structure and dynamics of the free/adsorbed protein and how these properties are altered upon single-point mutations. The results revealed that wild-type Azurin adsorbs on Au(111) along two well defined configurations: one tethered via cysteine groups and the other via the hydrophobic pocket surrounding the Cu 2 + . Surprisingly, our simulations revealed that single amino-acid mutations gave rise to a quenching of protein vibrations ultimately resulting in its overall stiffening. Given the role of amino-acid vibrations and reorientation in the dehydration process at the protein-water-substrate interface, we suggest that this might have an effect on the adsorption process of the mutant, giving rise to new adsorption configurations.
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