Structural Bioelectrochemistry of Membrane-Bound Dehydrogenases from Acetic Acid Bacteria

• Published in: BUNSEKI KAGAKU Vol. 74; no. 7.8; pp. 351 - 361
• Main Authors: ICHIKAWA, Konatsu, ADACHI, Taiki, SOWA, Keisei
• Format: Journal Article
• Language: Japanese
• Published: The Japan Society for Analytical Chemistry 05.07.2025
• Subjects: bioelectrocatalysis; cryo-electron microscopy; dehydrogenase; direct electron transfer
• ISSN: 0525-1931
• DOI: 10.2116/bunsekikagaku.74.351

Some dehydrogenases, derived from acetic acid bacteria, can directly transfer electrons to electrodes and couple enzymatic reactions with electrode reactions. The coupled reaction is called a direct electron transfer (DET)-type reaction and is expected to be used not only as a method for evaluating the basic electrochemical properties of enzyme functions but also in third-generation biosensors, next-generation biofuel cells, and bioreactors. Fructose dehydrogenase (FDH), alcohol dehydrogenase (ADH), and aldehyde dehydrogenase (ALDH) from acetic acid bacteria are membrane-bound proteins with outstanding DET activity and have been the subject of bioelectrochemical research. The three-dimensional structures of these enzymes have recently been analyzed thanks to the development of cryo-electron microscopy. Based on the elucidated three-dimensional structures, efforts to integrate the viewpoints of structural biology and bioelectrochemistry have been actively undertaken. In this paper, the research of FDH, ADH, and ALDH from acetic acid bacteria is outlined, and future prospects are also introduced.