Presentation Information

[17p-M_135-8]Enantioselective Adsorption of Metalloenzymes and Oxygen Reduction Activity at Amino Acid–Modified Au(111) Single Crystalline Electrodes

〇Sayuki Oka1, Masaru Kato2,3, Ryuto Ohashi4, Hisayoshi Matsushima4, Takahide Yamaguchi5, Aozora Sugai5, Shogo Hoshino3, Ichizo Yagi2,3 (1.RIES, Hokkaido Univ., 2.Faculty Env. Earth Sci., Hokkaido Univ., 3.Grad. School Env. Sci., Hokkaido Univ., 4.Grad. School Eng., Hokkaido Univ., 5.Grad. School Sci., Ibaraki Univ.)

Keywords:

oxygen reduction reaction,enantioselective adsorption,metalloenzyme

A metalloenzyme laccase was immobilized on amino acid–modified Au(111) single crystalline electrodes, and the effect of enantioselective adsorption of laccase on the oxygen reduction reaction (ORR) activity was investigated. The ORR current densities were found to depend on the chirality of the modifying amino acid. In contrast, when the current densities were normalized by the immobilization density, no difference was observed, indicating that the apparent activity difference originates from the difference in the amount of enantioselective adsorption.