Tuning Structure and Dynamics of Blue Copper Azurin Junctions via Single Amino-Acid Mutations

Biomolecules

卷:9

JuanCarlos Cuevas¹  LindaA. Zotti²  Rubén Pérez²  Maria Ortega²  J.G. Vilhena²  Ismael Díez-Pérez³ 

[1] Mathematical Sciences, King’s College London, Britannia House, 7 Trinity Street, London SE1 1DB, UK;

[2] Departamento de Física Teórica de la Materia Condensada, Universidad Autónoma de Madrid, E-28049 Madrid, Spain;

[3] Department of Chemistry, Faculty of Natural &

关键词: biomolecular electronics;    azurin;    single molecule;    solid-state junction;    molecular dynamics;    protein adsorption;    electronic transport;    single-point-mutation;   

DOI  :  10.3390/biom9100611

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown