Reflection anisotropy spectroscopy of decanethiol adsorbed at Au(110)/liquid interfaces

Bowfield, A.; Cm, Smith; Cuquerella, M. Consuelo; Farrell, T.; Fernig, David G.; Edwards, C.; Weightman, P.

doi:10.1002/pssc.200779111

Cited by 4 publications

(5 citation statements)

References 26 publications

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“…1) and those of the adsorbed protein occurs for the applied potential of 0.056 V. This difference is very likely to be due to the replacement of the weakly adsorbed anions on the Au(110)-buffer interface by the CPR which makes a strong Au-S bond with the Au(110) surface [5,6]. Previous work shows [20][21][22] that this bond is not disrupted by variations in the applied potential so the anions will not be able to return to the surface as the potential is varied. The main differences between the RAS profiles of the adsorbed proteins and the Au(110)-interface are a reduction in the intensity of the broad positive peak centered on ∼2.0 eV and an increased, negative, intensity in the region of 2.5 to 3.5 eV.…”

Section: Discussionmentioning

confidence: 90%

“…Although the adsorbed protein does not become completely reduced this trend is also observed in the RAS profiles of the protein on the Au(110) surface particularly when the potential dependence of the RAS peak arising from the Au-S bond is taken into account. Previous studies of the RAS of the Au-S bond formed on Au(110) at −0.6 V by cysteine, cystine [20], a cysteine-tryptophan dipeptide [21], and decanethiol [22] show that it contributes a symmetric peak located at 2.5 eV with a width of ∼0.3 eV at full width at half maximum. In the RAS of these smaller molecules [20,21] adsorbed on Au(110) this feature remains sharp but reduces in intensity by 50% when the applied potential is increased to 0.0 V. This intensity variation is opposite to the behavior shown in Fig.…”

Section: -3mentioning

confidence: 97%

“…As in previous work [7][8][9][20][21][22][23][24] we assume that the RAS of the adsorbed molecules is the sum of the contribution from the molecules and from the Au(110) surface together with the contribution from the Au-S bond. Figure 6 shows the difference between the RAS profiles of Figs.…”

Section: -3mentioning

confidence: 99%

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Conformational change induced by electron transfer in a monolayer of cytochrome P450 reductase adsorbed at the Au(110)–phosphate buffer interface

Weightman

et al. 2013

Phys. Rev. E

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The reflection anisotropy spectroscopy profiles of a variant of cytochrome P450 reductase adsorbed at the Au(110)-phosphate buffer interface depend on the sequence of potentials applied to the Au(110) electrode. It is suggested that this dependence arises from changes in the orientation of the isoalloxazine ring structures in the protein with respect to the Au(110) surface. This offers a method of monitoring conformational change in this protein by measuring variations in the reflection anisotropy spectrum arising from changes in the redox potential.

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Section: Discussionmentioning

confidence: 90%

Section: -3mentioning

confidence: 97%

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Conformational change induced by electron transfer in a monolayer of cytochrome P450 reductase adsorbed at the Au(110)–phosphate buffer interface

Weightman

et al. 2013

Phys. Rev. E

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“…Experience with small molecules, the S-containing amino acids [29], decanethiol [30], and a cysteine-tryptophan dimer [31], leads us to expect that the protein molecules ( Fig. 1) will adsorb through the formation of a Au(110)-S linkage and that this will lead to a characteristic Au-S peak in the RAS at ∼2.54 eV.…”

Section: Resultsmentioning

confidence: 98%

Controlling the formation of a monolayer of cytochrome P450 reductase onto Au surfaces

Convery

Khara

et al. 2012

Phys. Rev. E

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The conditions necessary for the formation of a monolayer and a bilayer of a mutated form (P499C) of human cytochrome P450 reductase on a Au(110)/electrolyte interface have been determined using a quartz crystal microbalance with dissipation, atomic force microscopy, and reflection anisotropy spectroscopy (RAS). The molecules adsorb through a Au-S linkage and, for the monolayer, adopt an ordered structure on the Au(110) substrate in which the optical axes of the dipoles contributing to the RAS signal are aligned roughly along the optical axes of the Au(110) substrate. Differences between the absorption spectrum of the molecules in a solution and the RAS profile of the adsorbed monolayer are attributed to surface order in the orientation of dipoles that contribute in the low energy region of the spectrum, a roughly vertical orientation on the surface of the long axes of the isoalloxazine rings and the lack of any preferred orientation in the molecular structure of the dipoles in the aromatic amino acids. Our studies establish an important proof of principle for immobilizing large biological macromolecules to gold surfaces. This opens up detailed studies of the dynamics of biological macromolecules by RAS, which have general applications in studies of biological redox chemistry that are coupled to protein dynamics.

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“…Understanding of the substrate surface at the atomic level and mapping of the substrate–molecule interaction at least to molecular scale are crucial. This has been achieved for Au–S linked S-containing molecules that form highly ordered self-assembled molecular monolayers (SAMs) and for redox metalloproteins and metalloenzymes in aqueous solution under electrochemical control. ,, Au(111)-electrode surfaces have been by far the most commonly used substrate, but binding and single-molecule EC-STM mapping of a protein (human insulin) on Au(100) and Au(110) have also recently been reported . On the other hand, pure and redox group modified oligonucleotides linked to polycrystalline Au-electrode surfaces have been extensively studied by electrochemical methods addressing long-range electron transfer along the double-strand axis .…”

Section: Introductionmentioning

confidence: 99%

DNA Bases Assembled on the Au(110)/Electrolyte Interface: A Combined Experimental and Theoretical Study

et al. 2015

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Among the low-index single-crystal gold surfaces, the Au(110) surface is the most active toward molecular adsorption and the one with fewest electrochemical adsorption data reported. Cyclic voltammetry (CV), electrochemically controlled scanning tunneling microscopy (EC-STM), and density functional theory (DFT) calculations have been employed in the present study to address the adsorption of the four nucleobases adenine (A), cytosine (C), guanine (G), and thymine (T), on the Au(110)-electrode surface. Au(110) undergoes reconstruction to the (1 × 3) surface in electrochemical environment, accompanied by a pair of strong voltammetry peaks in the double-layer region in acid solutions. Adsorption of the DNA bases gives featureless voltammograms with lower double-layer capacitance, suggesting that all the bases are chemisorbed on the Au(110) surface. Further investigation of the surface structures of the adlayers of the four DNA bases by EC-STM disclosed lifting of the Au(110) reconstruction, specific molecular packing in dense monolayers, and pH dependence of the A and G adsorption. DFT computations based on a cluster model for the Au(110) surface were performed to investigate the adsorption energy and geometry of the DNA bases in different adsorbate orientations. The optimized geometry is further used to compute models for STM images which are compared with the recorded STM images. This has provided insight into the physical nature of the adsorption. The specific orientations of A, C, G, and T on Au(110) and the nature of the physical adsorbate/surface interaction based on the combination of the experimental and theoretical studies are proposed, and differences from nucleobase adsorption on Au(111)- and Au(100)-electrode surfaces are discussed.

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Reflection anisotropy spectroscopy of decanethiol adsorbed at Au(110)/liquid interfaces

Cited by 4 publications

References 26 publications

Conformational change induced by electron transfer in a monolayer of cytochrome P450 reductase adsorbed at the Au(110)–phosphate buffer interface

Conformational change induced by electron transfer in a monolayer of cytochrome P450 reductase adsorbed at the Au(110)–phosphate buffer interface

Controlling the formation of a monolayer of cytochrome P450 reductase onto Au surfaces

DNA Bases Assembled on the Au(110)/Electrolyte Interface: A Combined Experimental and Theoretical Study

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