The Redox Potential Measurements for Heme Moieties in Variants of D-Fructose Dehydrogenase Based on Mediator-assisted Potentiometric Titration
The effect of mutation on the redox potentials (E°′) of the heme moieties in the variants of d-fructose dehydrogenase (FDH) was investigated by mediated spectroelectrochemical titrations. The replacement of the axial ligand of heme from methionine to glutamine changes the E°′ value more negatively t...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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The Electrochemical Society of Japan
2021-07-01
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| Series: | Electrochemistry |
| Subjects: | |
| Online Access: | https://www.jstage.jst.go.jp/article/electrochemistry/89/4/89_21-00044/_pdf/-char/en |
| Summary: | The effect of mutation on the redox potentials (E°′) of the heme moieties in the variants of d-fructose dehydrogenase (FDH) was investigated by mediated spectroelectrochemical titrations. The replacement of the axial ligand of heme from methionine to glutamine changes the E°′ value more negatively than that of the corresponding heme moiety in the recombinant (native) FDH (rFDH). The determined E°′ values of non-targeted heme moieties in the variants were also shifted in a negative direction from that in rFDH. Thus, enzyme modification changes E°′ of the heme moieties in unmodified protein regions. |
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| ISSN: | 2186-2451 |