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.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2006
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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.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2006
User Contributions:
Comment about this article or add new information about this topic:
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.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2004
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