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.

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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.

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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.

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