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J. Biochem, 1990, Vol. 107, No. 6 863-867
© 1990 Japanese Biochemical Society

research-article

Evidence for Electron Transfer via Ubiquinone between Quinoproteins D-Glucose Dehydrogenase and Alcohol Dehydrogenase of Gluconobacter suboxydans1

Emiko Shinagawa, Kazunobu Matsushita, Osao Adachi and Minoru Ameyama

Department of Agricultural Chemistry, Faculty of Agriculture, Yamaguchi University Yamaguchi, Yamaguchi 753

Gluconobacter suboxydans containso membrane-bound D-glucose and alcohol dehydro-genases (GDH and ADH) as the primary dehydrogenases in the respiratory chain. These enzymes are known to be quinoproteins having pyrroloquinoline quinone as the prosthetic group. GDH reduces an artificial electron acceptor, ferricyanide, in the membrane, but not after solubilization with Triton X-100, while ADH can react with the electron acceptor even after solubilization and further purification. In this study, it has been shown that the ferricyanide reductase activity of GDH is restored by adding the supernatant solubilized with Triton X-100 to the residue, and also by incorporation of purified ADH into the membranes of an ADH-deficient strain, G. suboxydans var. {alpha}. In addition, the ferricyanide reductase activity of GDH was reconstituted in proteoliposomes from GDH, ADH, and ubiquinone10. Thus, the results indicated that the electron transfer from GDH to ferricyanide was mediated by ubiquinone and ADH. The data also suggest that GDH and ADH transfer electrons mutually via ubiquinone in the respiratory chain.

1 This work was supported by a Grant-in-Aid (No. 62440014) for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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 J. Biol. Chem.Home page
K. Matsushita, T. Yakushi, H. Toyama, E. Shinagawa, and O. Adachi
Function of Multiple Heme c Moieties in Intramolecular Electron Transport and Ubiquinone Reduction in the Quinohemoprotein Alcohol Dehydrogenase-Cytochrome c Complex of Gluconobacter suboxydans
J. Biol. Chem., March 1, 1996; 271(9): 4850 - 4857.
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