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Redox State Control of Human Cytoglobin by Direct Electrochemical Method to Investigate Its Function in Molecular Basis.
- Source :
-
Chemical & pharmaceutical bulletin [Chem Pharm Bull (Tokyo)] 2020 Aug 01; Vol. 68 (8), pp. 806-809. Date of Electronic Publication: 2020 May 26. - Publication Year :
- 2020
-
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.
- Subjects :
- 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
Cytoglobin chemistry
Electrochemical Techniques methods
Subjects
Details
- Language :
- English
- ISSN :
- 1347-5223
- Volume :
- 68
- Issue :
- 8
- Database :
- MEDLINE
- Journal :
- Chemical & pharmaceutical bulletin
- Publication Type :
- Academic Journal
- Accession number :
- 32461519
- Full Text :
- https://doi.org/10.1248/cpb.c20-00175