Orientational control of the physiological reaction of cytochrome c oxidase tethered to a gold electrode

Article Abstract:

The functionality of a lipid-reconstituted recombinant cytochrome c oxidase (CcO) monolayer that is specifically bound through histidine tags (His-tags) to a nickel chelating nitrilotriacetic acid (Ni-NTA)-modified gold electrode is described. The method has shown that the orientation of the membrane protein can be controlled depending on the position of the affinity tag.

All Other Basic Organic Chemical Manufacturing, Industrial Organic Chemicals, Nitrilotriacetic Acid, Analysis, Infrared spectroscopy, ATP synthesis

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Orientational control of the physiological reaction of cytochrome c oxidase tethered to a gold electrode

Article Abstract:

The functionality of a lipid-reconstituted recombinant cytochrome c oxidase (CcO) monolayer that is specifically bound through histidine tags (His-tags) to a nickel chelating nitrilotriacetic acid (Ni-NTA)-modified gold electrode is described. The method has shown that the orientation of the membrane protein can be controlled depending on the position of the affinity tag.

Monomolecular films

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Redox-dependent pK(sub a) of Cu(sub B) histidine ligand in cytochrome c oxidase

Article Abstract:

The study used density functional theory to calculate the proton affinity of the delta-nitrogen of His291, and used the self-consistent reaction field method to calculate the solvation energies. Using the minimal model, it obtained aqueous phase pK(sub a)'s for the His 291 residue of 9 and 13 with oxidized and reduced Cu(sub B) respectively.

Oxidation-reduction reaction, Oxidation-reduction reactions

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