Electron Transfer Reactions of Semi-Artificial Biomolecules
Using functional electrodes electrochemical responses of semi-artificially modified myoglobin and ferredoxin molecules have been examined to understand biological functions in more detail. Some reconstituted myoglobin molecules of which redox center was changed with artificially designed porphyrins showed that for determining the redox potential axial ligands are important when the porphyrin is incorporated inside the apomyoglobin. Change in metal ion of the redox center gave significant change in the electron transfer rate. For ferredoxin some evolutionary-conserved amino acid residues were changed to understand the roles of the amino acid ion biological functions using mutated molecules, and some particular amino acid residues were found to have distinguished roles in biological functions such as controlling the redox potential and as the binding site with enzymes.
KeywordsRedox Potential Electron Transfer Reaction Electron Transfer Rate Redox Center Electron Transfer Rate Constant
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