Catalytic monolayer voltammetry and in situ scanning tunneling microscopy of copper nitrite reductase on cysteamine-modified Au(111) electrodes

Article Abstract:

Studies done on the adsorption and electrocatalysis of the redox metalloenzyme blue copper nitrite reductase from Achromobacter xylosoxidans (AxCuNiR) on single-crystal Au(111)-electrode surfaces modified by a highly ordered self-assembled monolayer of cysteamine is presented. Studies demonstrate that AxCuNiR can be brought to immobilization in a functional state on suitably modified, well defined, atomically planar Au(111)-electrode surfaces.

Chemistry, Physical and theoretical, Physical chemistry, Scanning tunneling microscopy, Adsorption, Copper compounds, Atomic properties

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Coexistence of multiple conformations in cysteamine monolayers on Au(111)

Article Abstract:

The structural organization, catalytic function, and electronic properties of cysteamine monolayers on Au(111) is addressed comprehensively by voltammetry, in situ scanning tunneling microscopy (STM) in anaerobic environment, and a priori molecular dynamics (MD) simulation and STM image simulation. It is concluded that the adsorbate surface is controlled by interactions with the solvent rather than with the substrate.

Observations, Monomolecular films, Cysteamine

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Ordered assembly and conrtolled electron transfer of the blue copper protein azurin at gold (111) single-crystal substrates

Article Abstract:

Ordered protein assembly, high stability and sensitivity and fast controllable electronic transfer is indicated. These properties can hold a perspective for electronic mapping of single redox protein molecules.

Analysis, Pseudomonas aeruginosa, Optical properties, Charge transfer

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