The Redox Potential Measurements for Heme Moieties in Variants of D-Fructose Dehydrogenase Based on Mediator-assisted Potentiometric Titration

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...

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Main Authors: Yohei SUZUKI, Keisei SOWA, Yuki KITAZUMI, Osamu SHIRAI
Format: Article
Language:English
Published: The Electrochemical Society of Japan 2021-07-01
Series:Electrochemistry
Subjects:
d-fructose dehydrogenase
potentiometric titration
heme moieties
mutations
Online Access:https://www.jstage.jst.go.jp/article/electrochemistry/89/4/89_21-00044/_pdf/-char/en
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spelling doaj-9d4118d881c84233ba3d4da28c5c7e072021-09-02T04:54:44ZengThe Electrochemical Society of JapanElectrochemistry2186-24512021-07-0189433733910.5796/electrochemistry.21-00044electrochemistryThe Redox Potential Measurements for Heme Moieties in Variants of D-Fructose Dehydrogenase Based on Mediator-assisted Potentiometric TitrationYohei SUZUKI0Keisei SOWA1Yuki KITAZUMI2Osamu SHIRAI3Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto UniversityDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto UniversityDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto UniversityDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto UniversityThe 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.https://www.jstage.jst.go.jp/article/electrochemistry/89/4/89_21-00044/_pdf/-char/end-fructose dehydrogenasepotentiometric titrationheme moietiesmutations
collection DOAJ
language English
format Article
sources DOAJ
author Yohei SUZUKI
Keisei SOWA
Yuki KITAZUMI
Osamu SHIRAI
spellingShingle Yohei SUZUKI
Keisei SOWA
Yuki KITAZUMI
Osamu SHIRAI
The Redox Potential Measurements for Heme Moieties in Variants of D-Fructose Dehydrogenase Based on Mediator-assisted Potentiometric Titration
Electrochemistry
d-fructose dehydrogenase
potentiometric titration
heme moieties
mutations
author_facet Yohei SUZUKI
Keisei SOWA
Yuki KITAZUMI
Osamu SHIRAI
author_sort Yohei SUZUKI
title The Redox Potential Measurements for Heme Moieties in Variants of D-Fructose Dehydrogenase Based on Mediator-assisted Potentiometric Titration
title_short The Redox Potential Measurements for Heme Moieties in Variants of D-Fructose Dehydrogenase Based on Mediator-assisted Potentiometric Titration
title_full The Redox Potential Measurements for Heme Moieties in Variants of D-Fructose Dehydrogenase Based on Mediator-assisted Potentiometric Titration
title_fullStr The Redox Potential Measurements for Heme Moieties in Variants of D-Fructose Dehydrogenase Based on Mediator-assisted Potentiometric Titration
title_full_unstemmed The Redox Potential Measurements for Heme Moieties in Variants of D-Fructose Dehydrogenase Based on Mediator-assisted Potentiometric Titration
title_sort redox potential measurements for heme moieties in variants of d-fructose dehydrogenase based on mediator-assisted potentiometric titration
publisher The Electrochemical Society of Japan
series Electrochemistry
issn 2186-2451
publishDate 2021-07-01
description 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.
topic d-fructose dehydrogenase
potentiometric titration
heme moieties
mutations
url https://www.jstage.jst.go.jp/article/electrochemistry/89/4/89_21-00044/_pdf/-char/en
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