C-terminal Periplasmic Domain of Escherichia coli Quinoprotein Glucose Dehydrogenase Transfers Electrons to Ubiquinone

• Published in: The Journal of biological chemistry Vol. 276; no. 51; pp. 48356 - 48361
• Main Authors: Elias, MD, Tanaka, Makoto, Sakai, Masayoshi, Toyama, Hirohide, Matsushita, Kazunobu, Adachi, Osao, Yamada, Mamoru
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 21.12.2001
• Subjects: Amino Acid Sequence; Base Sequence; beta-Lactamases - metabolism; DNA Primers; Electron Transport; Escherichia coli; Escherichia coli - enzymology; Evolution, Molecular; Genetic Complementation Test; glucose dehydrogenase; Glucose Dehydrogenases - chemistry; Glucose Dehydrogenases - genetics; Glucose Dehydrogenases - isolation & purification; Glucose Dehydrogenases - metabolism; Glucose Oxidase - metabolism; Kinetics; Molecular Sequence Data; Periplasm - enzymology; Recombinant Fusion Proteins - metabolism; ubiquinol oxidase; ubiquinone; Ubiquinone - metabolism

Membrane-bound quinoprotein glucose dehydrogenase (GDH) in Escherichia coli donates electrons directly to ubiquinone during the oxidation of d-glucose as a substrate, and these electrons are subsequently transferred to ubiquinol oxidase in the respiratory chain. To determine whether the specific ubi...