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Characterization of Enzymes Against Oxygen Derivatives Produced by Rhodobacter sphaeroides D-230  

김동식 (동아대학교 자연과학대학 화학 생명과학부 생명과학전공)
이혜주 (동아대학교 자연과학대학 화학 생명과학부 생명과학전공)
Publication Information
Korean Journal of Microbiology / v.40, no.2, 2004 , pp. 94-99 More about this Journal
Abstract
The activities of enzymes that act on oxygen derivatives in Rhodobacter sphaeroides D-230 were investigated under various culture conditions. Intracellular SOD activity from the cells grown in aerobic or anaerobic culture conditions was highest at pH 7.0 and pH 8.0, respectively. On the other hand, extracellular SOD activity was highest at pH 6.0. Catalase activity was highest at neutral pH in both cases. Growth of R. sphaeroides D-230 in aerobic or anaerobic culture conditions was inhibited by methyl viologen. As R. sphaeroides D-230 was cul-tured aerobically, SOD activity was increased about 2-fold by addition of iron ion. But $Mn^+2$ had little effect on the SOD activity of R. sphaeroides D-230 grown in aerobically. NaCN, the inhibitor of Cu$.$Zn-SOD, did not inhibit SOD activity. But, $NaN_3$, the inhibitor of Mn-SOD, inhibited SOD activity in anaerobic cultures con-dition. Therefore, R. sphaeroides D-230 produce Mn-SOD in anaerobic condition, although Fe-Sod is produced in aerobic condition. The activity of catalase was induced by methyl viologen, however, extremely inhibited by NaCN and $NaN_3$.
Keywords
catalase; methyl viologen; photosynthetic bacteria; Rhodobacter sphaeroides D-230; superoxide dismutase (SOD);
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