A Tightly Bound Quinone Functions in the Ubiquinone Reaction Sites of Quinoprotein Alcohol Dehydrogenase of an Acetic Acid Bacterium, Gluconobacter suboxydans
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概要
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Quinoprotein alcohol dehydrogenase (ADH) of acetic acid bacteria is a membrane-bound enzyme that functions as the primary dehydrogenase in the ethanol oxidase respiratory chain. It consists of three subunits and has a pyrroloquinoline quinone (PQQ) in the active site and four heme c moieties as electron transfer mediators. Of these, three heme c sites and a further site have been found to be involved in ubiquinone (Q) reduction and ubiquinol (QH2) oxidation respectively (Matsushita et al., Biochim. Biophys. Acta, 1409, 154–164 (1999)). In this study, it was found that ADH solubilized and purified with dodecyl maltoside, but not with Triton X-100, had a tightly bound Q, and thus two different ADHs, one having the tightly bound Q (Q-bound ADH) and Q-free ADH, could be obtained. The Q-binding sites of both the ADHs were characterized using specific inhibitors, a substituted phenol PC16 (a Q analog inhibitor) and antimycin A. Based on the inhibition kinetics of Q2 reductase and ubiquinol-2 (Q2H2) oxidase activities, it was suggested that there are one and two PC16-binding sites in Q-bound ADH and Q-free ADH respectively. On the other hand, with antimycin A, only one binding site was found for Q2 reductase and Q2H2 oxidase activities, irrespective of the presence of bound Q. These results suggest that ADH has a high-affinity Q binding site (QH) besides low-affinity Q reduction and QH2 oxidation sites, and that the bound Q in the QH site is involved in the electron transfer between heme c moieties and bulk Q or QH2 in the low-affinity sites.
著者
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TOYAMA Hirohide
Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University
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MATSUSHITA Kazunobu
Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University
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ADACHI Osao
Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University
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KOBAYASHI Yoshiki
Department of Physiology, Hyogo College of Medicine
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Mizuguchi Mitsuhiro
Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University
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SAKAMOTO Kimitoshi
Department of Biomedical Chemistry, Graduate School of Medicine, The University of Tokyo
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MIYOSHI Hideto
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
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Murata Kousaku
Dep. Of Basic And Applied Molecular Biotechnology Div. Of Food And Biological Sci. Graduate School O
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Momma Keiko
Laboratory Of Basic And Applied Molecular Biotechnology Graduate School Of Agriculture Kyoto Univers
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Matsushita K
Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University
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