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Chem Pharm Bull (Tokyo) ; 68(8): 806-809, 2020 Aug 01.
Article in English | MEDLINE | ID: mdl-32461519

ABSTRACT

The direct electron transfer between human cytoglobin (Cygb) and the electrode surface, which would allow manipulating the oxidation states of the heme iron in Cygb, was first observed by immobilizing Cygb on a nanoporous gold (NPG) electrode via a carboxy-terminated alkanethiol. The voltammetric performances of the wild type and mutated Cygb-immobilized NPG electrodes were evaluated in the absence or presence of potential substrates. The obtained results demonstrated that the usefulness of the proposed method in understanding the function of Cygb in molecular basis.


Subject(s)
Cytoglobin/chemistry , Electrochemical Techniques/methods , Cytoglobin/genetics , Cytoglobin/metabolism , Electrodes , Electron Transport , Gold/chemistry , Humans , Hydrogen Peroxide/chemistry , Kinetics , Mutagenesis, Site-Directed , Nanopores , Oxidation-Reduction , Recombinant Proteins/biosynthesis , Recombinant Proteins/chemistry , Recombinant Proteins/isolation & purification
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