NADPH Oxidase System as a Superoxide-generating Cyanide-Resistant Pathway in the Respiratory Chain of Corynebacterium glutamicum

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概要

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• The respiratory chain of Corynebacterium glutamicum was investigated, especially with respect to a cyanideresistant respiratory chain bypass oxidase. The membranes of C. glutamicum had NADH, succinate, lactate, and NADPH oxidase activities, and menaquinone, and cytochromes a_<598>, b_<562(558)>, and c_<550> as respiratory components. The NADH, succinate, lactate, and NADPH oxidase systems, all of which were more cyanide-resistant than N, N, N', N'-tetramethyl-p-phenylene diamine oxidase activity (cytochrome aa_3 terminal oxidase), had different sensitivities to cyanide ; the cyanide sensitivity of these oxidase systems increased in the order, NADPH, lactate, NADH, and succinate. Taken together with the analysis of redox kinetics in the cytochromes and the effects of respiratory inhibitors, the results suggested that there is a cyanide-resistant bypass oxidase branching at the menaquinone site, besides cyanide-sensitive cytochrome oxidase in the respiratory chain. H^+/O measurements with resting cells suggested that the cyanide-sensitive respiratory chain has two or three coupling sites, of which one is in NADH dehydrogenase and the others between menaquinone and cytochrome oxidase, but the cyanide-resistant bypass oxidase may not have any proton coupling site. NADPH and lactate oxidase systems were more resistant to UV irradiation than other systems and the UV insensitivity was highest in the NADPH oxidase system, suggesting that a specific quinone resistant to UV or no such a quinone works in at least NADPH oxidase system while the UV-sensitive menaquinone pool does in other oxidase systems. Furthermore, superoxide was generated in well-washed membranes, most strongly in the NADPH oxidase system. Thus, it was suggested that the cyanide-resistant bypass oxidase system of C. glutamicum is related to the NADPH oxidase system, which may be involved in generation of superoxide anions and probably functions together with superoxide dismutase and catalase.

• 1998-10-23

著者

• TOYAMA Hirohide

  Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University

• MATSUSHITA Kazunobu

  Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University

• ADACHI Osao

  Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University

• Toyama Hirohide

  Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University

• Adachi Osao

  Derartment Of Blological Chemistry Faculty Of Agriculture Yamaguchi University

• Adachi Osao

  Department Of Agricultural Chemistry Yamaguchi University

• Yamamoto T

  Nara Inst. Sci. And Technol. Nara

• YAMAMOTO Toshinobu

  Department of Pathology, Sapporo Medical University School of Medicine

• Matsushita Kazunobu

  Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University

• Yamamoto Toshinobu

  Department Of Biological Chemistry Faculty Of Agriculture Yamaguchi University

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