Ford, M. J.

Hush, N. S.

Marcuccio, S.

Reimers, J. R.

Ulstrup, Jens

Zhang, Jingdong

Interfacial electrochemical electron transfer (ET) of redox metalloproteins is long established. For the proteins to retain full ET or enzyme activity, modification of the electrode surfaces, such as goldsurfaces by self-assembled molecular monolayers (SAMs), is nearly always required, where pure and functionalized alkanethiols have emerged as core linkers. We overview first binding and single-molecule long-range electron transfer of some metalloproteins, metalloenzymes, and DNA-based molecules on single-crystal Au(111), Au(100), and Au(100) electrode surfaces, bound either directly by Au-S linking of surface cysteines to the gold surfaces, or indirectly by non-covalent linking to SAMs of pure and functionalized alkanethiols. Core techniques are electrochemistry, surface spectroscopies, and in situ STM and AFM under electrochemical potential control, framed by single-molecule charge transport theory and electronic structure computations. Molecular packing, voltammetry and in situ STM/AFM are found to be exceedingly sensitive to the structure of the thiol-based SAM molecules, testifying both to the crucial importance of the Au-S binding, and to the SAM linking to the protein. A primary focus that has emerged is the electronic structure of the Au-S link and the packing of the SAMs. We have, first disentangled a wealth of data to identify the nature of the core Au-S contact. All data suggest that the electronic Au-S link is dominated by a Au(0)-thiyl radical with strong vander Waals forces and not by a Au(I)-thiolate ionic/covalent unit. Molecular packing is, further crucially determined by the SAM molecular structure and involves binding either to Au-atoms mined out of the surface or directly to a flat single-crystal surface. We illustrate this by high-resolution in situ STM of straight, branched, and chiral alkanethiols on Au(111)-electrode surfaces

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R.; Ulstrup, Jens; Zhang, JingdongPublication date:2017Document VersionPublisher's PDF, also known as Version of recordLink back to DTU OrbitCitation (APA):Ford, M. J., Hush, N. S., Marcuccio, S., Reimers, J. R., Ulstrup, J., & Zhang, J. (2017). The Au-S bond inbiomolecular adsorption and electrochemical electron transfer. Abstract from 2nd Gerischer-Kolb Symposium,Günzburg/Donau , Germany.  1 The Au-S bond in biomolecular adsorption and electrochemical electron transfer  M.J. Ford1, N.S. Hush2,3, S. Marcuccio4,5, J.R. Reimers1,6, Jens Ulstrup7*, and J. Zhang7,   1School of Mathematical and Physical Sci., Univ. of Technology of Sydney, NSW 2007, Australia. 2School of Chemistry F11, and 3School of Molecular Biosci., Univ. of Sydney, NSW 2006, Australia. 4Dept. Chem. and Phys., La Trobe Inst. for Mol. Sci., La Trobe Univ., Melbourne, Victoria 3086, Australia, and 5Advanced Molecular Technologies Pty Ltd. Unit 1, Victoria 3179, Australia. 6Int. Centre for Quantum and Molecular Structure, College of Sci., Shanghai Univ., 200444 China 7Department of Chemistry, Technical Univ. of Denmark, 2800 Lyngby, Denmark. *ju@kemi.dtu.dk   Interfacial electrochemical electron transfer (ET) of redox metalloproteins is long established1. For the proteins to retain full ET or enzyme activity, modification of the electrode surfaces, such as gold surfaces by self-assembled molecular monolayers (SAMs), is nearly always required, where pure and functionalized alkanethiols have emerged as core linkers.  We overview first binding and single-molecule long-range electron transfer of some metalloproteins, metalloenzymes, and DNA-based molecules on single-crystal Au(111), Au(100), and Au(100) electrode surfaces, bound either directly by Au-S linking of surface cysteines to the gold surfaces, or indirectly by non-covalent linking to  SAMs of pure and functionalized alkanethiols1,2. Core techniques are electrochemistry, surface spectroscopies, and in situ STM and AFM under electrochemical potential control, framed by single-molecule charge transport theory and electronic structure computations3,4. Molecular packing, voltammetry and in situ STM/AFM are found to be exceedingly sensitive to the structure of the thiol-based SAM molecules, testifying both to the crucial importance of the Au-S binding, and to the SAM linking to the protein2-5. A primary focus that has emerged is the electronic structure of the Au-S link and the packing of the SAMs3,4. We have, first disentangled a wealth of data to identify the nature of the core Au-S contact. All data suggest that the electronic Au-S link is dominated by a Au(0)-thiyl radical with strong van der Waals forces and not by a Au(I)-thiolate ionic/covalent unit. Molecular packing is, further crucially determined by the SAM molecular structure and involves binding either to Au-atoms mined out of the surface or directly to a flat single-crystal surface. We illustrate this by high-resolution in situ STM of straight, branched, and chiral alkanethiols on Au(111)-electrode surfaces.  [1] J. Zhang, A.M. Kuznetsov, I.G. Medvedev, Q. Chi, T. Albrecht, P.S. Jensen and J. Ulstrup,  “Single-molecule Electron Transfer in Electrochemical Environments”, Chem. Rev. 108  (2008) 2737-2791.   [2] P. Salvatore, D. Zeng, K.K. Karlsen, Q. Chi, J. Wengel and J. Ulstrup, "Electrochemistry  of  single metalloprotein and DNA-based molecules at Au(111)-electrode surfaces",  ChemPhysChem 14 (2013) 2101-2111. [3] J.R. Reimers, M.J. Ford, A. Halder, J. Ulstrup, and N.S. Hush, "Gold surfaces and  nanoparticles are protected by Au(0)-thiyl species and are destroyed when Au(I)-thiolates  form", Proc. Nat. Acad. Sci. USA 113 (2016) E1424-E1433. [4] Q. Chi, M.J.  Ford, A. Halder, N.S.  Hush, J.R.  Reimers and J. Ulstrup, “Sulfur ligand  mediated electrochemistry of gold surfaces and nanoparticles:  what, how, and why?”,  Curr.  Opin. Electrochemistry 1 (2017) 7-15. [5] N. Zhu, J. Ulstrup and Q. Chi, “Long-range interfacial electron transfer and electrocatalysis  of  molecular scale Prussian Blue nanoparticles linked to Au(111)- electrode surfaces by  different chemical contacting groups”, Russ. J. Electrochemistry 53 (2017) in press. 

The Au-S bond in biomolecular adsorption and electrochemical electron transfer

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The Au-S bond in biomolecular adsorption and electrochemical electron transfer

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