Electrochemistry
Online ISSN : 2186-2451
Print ISSN : 1344-3542
ISSN-L : 1344-3542
CORRECTED PROOF
The Redox Potential Measurements for Heme Moieties in Variants of d-Fructose Dehydrogenase Based on Mediator-assisted Potentiometric Titration
Yohei SUZUKIKeisei SOWAYuki KITAZUMIOsamu SHIRAI
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JOURNALS OPEN ACCESS Advance online publication
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Article ID: 21-00044

CORRECTED PROOF: June 04, 2021
UNCORRECTED PROOF: May 25, 2021
ACCEPTED MANUSCRIPT: May 12, 2021
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Abstract

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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© The Author(s) 2021. Published by ECSJ.

This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 License (CC BY, http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse of the work in any medium provided the original work is properly cited. [DOI: 10.5796/electrochemistry.21-00044].
http://creativecommons.org/licenses/by/4.0/
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