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...

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Published inDenki kagaku oyobi kōgyō butsuri kagaku Vol. 89; no. 4; pp. 337 - 339
Main Authors KITAZUMI, Yuki, SHIRAI, Osamu, SUZUKI, Yohei, SOWA, Keisei
Format Journal Article
LanguageEnglish
Published Tokyo The Electrochemical Society of Japan 05.07.2021
Japan Science and Technology Agency
Subjects
D-Fructose Dehydrogenase
Dehydrogenase
Dehydrogenases
Fructose
Glutamine
Heme
Heme Moieties
Methionine
Mutation
Mutations
Potentiometric Titration
Redox potential
Titration
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ISSN1344-3542
2186-2451
DOI10.5796/electrochemistry.21-00044

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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:1344-3542
2186-2451
DOI:10.5796/electrochemistry.21-00044