日本語フィールド
著者：Masato Tominaga, Shiho Tamai, Shino Nakao, Miwa Miyamoto and Takenori Satomura題名：High electrochemical stability of hyperthermophilic archaeal multicopper enzyme adsorbed on gold electrodes compared to fungal laccase発表情報：Electrochemistry Communications 巻: 136 ページ: article No. 107222キーワード：概要：抄録：Multicopper enzymes (MCEs) have attracted significant recent attention for use as biocathodes in enzymecatalyzed
fuel cells, mostly to facilitate the four-electron reduction of oxygen to water. Au is highly biocompatible
and does not exhibit a carbon-like tendency for toxicity. Especially, the development of an implant-type
enzyme fuel cells with noble electrodes, such as those made of Au, can assist in resolving health issues. In the
present research, a direct electron transfer (DET)-type reaction featuring a hyperthermophilic archaeon multicopper
enzyme (McoP) and a Trametes sp. laccase (Lac) adsorbed on bare Au electrodes was investigated. Quartz
crystal microbalance (QCM) analysis was used to examine the adsorption behavior of McoP and Lac on Au
electrodes. The obtained results indicated that the adsorbed McoP on Au exhibited stability against a higher
potential electric field (+0.8 V vs. Ag|AgCl) and showed stable bioelectrocatalysis for oxygen reduction (main
production of H2O2 with two-electron reaction), compared with Lac. The electron transfer rate of the McoP at the
Au electrode interface was evaluated to be 10 s 1. This finding could urgently contribute for developing biocathodes
in enzyme-catalyzed fuel cell, especially implant-type enzymatic fuel cells.英語フィールド
Author：Masato Tominaga, Shiho Tamai, Shino Nakao, Miwa Miyamoto and Takenori SatomuraTitle：High electrochemical stability of hyperthermophilic archaeal multicopper enzyme adsorbed on gold electrodes compared to fungal laccaseAnnouncement information:Electrochemistry Communications Vol: 136 Page: article No. 107222An abstract：Multicopper enzymes (MCEs) have attracted significant recent attention for use as biocathodes in enzymecatalyzed
fuel cells, mostly to facilitate the four-electron reduction of oxygen to water. Au is highly biocompatible
and does not exhibit a carbon-like tendency for toxicity. Especially, the development of an implant-type
enzyme fuel cells with noble electrodes, such as those made of Au, can assist in resolving health issues. In the
present research, a direct electron transfer (DET)-type reaction featuring a hyperthermophilic archaeon multicopper
enzyme (McoP) and a Trametes sp. laccase (Lac) adsorbed on bare Au electrodes was investigated. Quartz
crystal microbalance (QCM) analysis was used to examine the adsorption behavior of McoP and Lac on Au
electrodes. The obtained results indicated that the adsorbed McoP on Au exhibited stability against a higher
potential electric field (+0.8 V vs. Ag|AgCl) and showed stable bioelectrocatalysis for oxygen reduction (main
production of H2O2 with two-electron reaction), compared with Lac. The electron transfer rate of the McoP at the
Au electrode interface was evaluated to be 10 s 1. This finding could urgently contribute for developing biocathodes
in enzyme-catalyzed fuel cell, especially implant-type enzymatic fuel cells.