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Gram-positive Bacillus cereus KCTC 3674와 Gram-negative Vibrio sp. KYJ 962의 호기성 호흡쇄의 NADH oxidase system에 관한 비교연구 원문보기
Studies on the aerobic respiratory chain-linked NADH oxidase system of Gram-positive Bacillus cereus KCTC 3674 and Gram-negative Vibrio sp. KYJ 962

  • 저자

    김만숙

  • 학위수여기관

    昌原大學校 大學院

  • 학위구분

    국내석사

  • 학과

    생물·미생물학과

  • 지도교수

  • 발행년도

    2003

  • 총페이지

    v, 61p.

  • 키워드

    Gram-positive Bacillus cereus KCTC 3674 Gram-negative Vibrio sp KYJ 962 호기성 호흡쇄 NADH oxidase system;

  • 언어

    kor

  • 원문 URL

    http://www.riss.kr/link?id=T9465933&outLink=K  

  • 초록

    Inverted membrane vesicles prepared from Bacillus cereus KCTC 3674 oxidized NADH, but very little deamino-NADH as a substrate. The maximum activity of membrane-bound NADH oxidase was obtained at about pH 8.5 in the presence of 0.1 M KCl (or NaCl). It exhibited an apparent K_(m) value of approximately 65 μM for NADH. Respiratory inhibitor HQNO inhibited the NADH oxidase activity by about 90% at a concentration of 40 μM. Rotenone and capsaicin also inhibited the activity by about 65% and 75% at a concentration of 100 μM and 300 μM, respectively. Interestingly, the NADH oxidase activity was highly sensitive to Ag^(+). On the other hand, the NADH:ubiquinone-1, NADH:ferricyanide, NADH:menadione, NADH:DCPIP oxidoreductase of the NADH oxidase system were quite different in the enzymatic properties from each other. NADH oxidase and deamino-NADH oxidase of Vibrio sp. KYJ 962 were stimulated by Na^(+), K^(+) and Li^(+). In the presence of NADH or deamino-NADH as electron donors, NADH oxidase system was approximately 4 fold higher in Na^(+) than K^(+) and Li^(+). The maximum activites of membrane-bound NADH oxidase and deamino-NADH oxidase were obtained at about pH 9.0 in the presence of 0.2 M NaCl. Respiratory inhibitor HQNO inhibited the NADH oxidase activity by about 97% at a concentration of 100 μM. Rotenone and capsaicin also inhibited the activity by about 20% and 35% at a concentration of 40 μM and 300 μM, respectively. The maximum activity of membrane-bound NADH:ubiquinone oxidoreductase was obtained at about pH 5.0 in the absence of NaCl. The optimal NaCl concentration for the activity was 0.2 M NaCl at pH 4.5, 8.5 and 9.0, 0.05 M NaCl at pH 5.0, and 0.1 M NaCl at pH 5.5. Respiratory inhibitor HQNO inhibited the NADH:ubiquinone oxidoreductase activity by about 55% at a concentration of 100 μM. Rotenone and capsaicin also inhibited the activity by about 10% and 35% at a concentration of 40 μM and 300 μM, respectively. Electron transfer from NADH to ubiquinone-1 generated a membrane potential (Δψ) was larger in the presence Na+ than that observed in the absence of Na^(+). The membrane potential was collapsed about 63% by 20 μM CCCP, and almost completely collapsed by 10 μM CCCP and 20 μM monensin. The membrane potential was almost completely inhibited by 40 μM HQNO and 300 μM capsaicin, and approximately 19% inhibited by 100 μM rotenone.


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