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| ファイル | 記述 | サイズ | フォーマット | |
|---|---|---|---|---|
| electrochemistry.21-00044.pdf | 1.26 MB | Adobe PDF | 見る/開く |
| タイトル: | The Redox Potential Measurements for Heme Moieties in Variants of d-Fructose Dehydrogenase Based on Mediator-assisted Potentiometric Titration |
| 著者: | SUZUKI, Yohei SOWA, Keisei    https://orcid.org/0000-0001-9767-4922 (unconfirmed)KITAZUMI, Yuki https://orcid.org/0000-0001-6171-6457 (unconfirmed)SHIRAI, Osamu |
| 著者名の別形: | 鈴木, 洋平 宋和, 慶盛 北隅, 優希 白井, 理 |
| キーワード: | D-Fructose Dehydrogenase Potentiometric Titration Heme Moieties Mutations |
| 発行日: | 5-Jul-2021 |
| 出版者: | The Electrochemical Society of Japan |
| 誌名: | Electrochemistry |
| 巻: | 89 |
| 号: | 4 |
| 開始ページ: | 337 |
| 終了ページ: | 339 |
| 抄録: | The effect of mutation on the redox potentials (E degrees') 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 degrees' value more negatively than that of the corresponding heme moiety in the recombinant (native) FDH (rFDH). The determined E degrees' 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 degrees' of the heme moieties in unmodified protein regions. (C) The Author(s) 2021. Published by ECSJ. |
| 著作権等: | © 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. |
| URI: | http://hdl.handle.net/2433/276527 |
| DOI(出版社版): | 10.5796/electrochemistry.21-00044 |
| 出現コレクション: | 学術雑誌掲載論文等 |
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