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Single molecule voltammetry

In a series of voltammetric experiments on nanoscale dendrimers, C. Ama-tore et al. discussed interesting nanoscale effects in single molecule voltammetry [ChemPhysChem 2 (2001) 130]. Fourth-generation PAMAM (polyamidoamide) dendrimers modified with 64 Ru(II) redox sites at their surface were adsorbed onto a platinum substrate the dendrimer molecule has a radius of approximately 5 nm (see Fig. 11.2). [Pg.239]

In Situ Imaging of Bio-related Molecules and Linker Molecules for Protein Voltammetry with Single-Molecule and Sub-molecular Resolution... [Pg.97]

Electrochemically controlled SAMs of the alkanethiol class characterized to high voltammetric resolution and to molecular and sub-molecular structural in situ STM resolution have been reviewed recently [60, 151]. We note here first some issues of importance to functionalized alkanethiols as linker molecules for gentle immobilization of fully functional redox metalloprotein monolayers on singlecrystal Au(lll) electrode surfaces. We discuss next specifically the functionalized alkanethiols cysteine (Cys) and homocysteine (Hey). These two molecules represent a core protein building block and a core metabolite, respectively. The former has been used to display unique sub-molecular in situ STM resolution [152]. The latter shows a unique dual surface dynamics pattern that could be followed both by single-molecule in situ STM and by high-resolution capacitive voltammetry. [Pg.100]

Butt and coworkers studied the voltammetry of the (Escherichia coli) decaheme class of nitrite reductases [244] (Figure 2.13). Well-defined although unstable catalytic multi-electron voltammetric reduction of nitrite by the enzyme immobihzed on bare Au(lll) electrode surfaces is notable. The decaheme nitrite reductase is a second case for single-molecule in situ STM of a redox metalloenzyme, but image interpretation is presently not at the level for CuNiR [227]. Molecular-scale structures can be observed on the Au(lll) electrode surface under conditions where the enzyme is electrocatalytically active, with both the natural dimer and surface-dissociated monomer enzyme structures identified. Molecular conductivities (in situ STM contrasts) of the enzyme and the active enzyme-substrate states are, however, not very distinctive. [Pg.120]

Overall the single-crystal voltammetry, surface promoter sensitivity, and in situ STM of PJ d illuminate procedures and approaches to highly increased resolution in the bioelectrochemical mapping of redox metalloproteins, approaching the electrochemical resolution of small molecular adsorbate molecules. [Pg.289]

The complexation behavior of SAMs of P-CD 1 was measured by single molecule force spectroscopy (Figure 4). Gold-coated AFM tips were modified with a mixed SAM of 2-hydroxy-ethanethiol and 6-ferrocenyl-hexanethiol. As shown by cyclic voltammetry experiments the mixed SAMs contained 1 % - 2 % 6-ferrocenyl-hexanethiol. The dilution was carried out in order to reduce the number of possible interactions and to maximize the conformational freedom of the immobilized ferrocene moieties. [Pg.117]

Thus, it would be expected that this compound would show two reduction peaks by cyclic voltammetry the first process should be reduction of aa and the second reduction of ee. However, at room temperature, only a single reduction peak is seen because the rate of interconversion of the two forms is so rapid that the entire population of reactant molecules near the electrode is reduced via the more easily reduced conformation, aa. [Pg.495]


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See also in sourсe #XX -- [ Pg.239 ]




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