Oxidations of various substrates and effects of the inhibitors on purified mitochondria isolated from Kalanchoë pinnata

H. T.K. Hong, A. Nose, S. Agarie

研究成果: Contribution to journalArticle査読

4 被引用数 (Scopus)

抄録

Kalanchoë pinnata mitochondria readily oxidized succinate, malate, NADH, and NADPH at high rates and coupling. The highest respiration rates usually were observed in the presence of succinate. The high rate of malate oxidation was observed at pH 6.8 with thiamine pyrophosphate where both malic enzyme (ME) and pyruvate dehydrogenase were activated. In CAM phase III of K. pinnata mitochondria, both ME and malate dehydrogenase (MDH) simultaneously contributed to metabolism of malate. However, ME played a main function: malate was oxidized via ME to produce pyruvate and CO2 rather than via MDH to produce oxalacetate (OAA). Cooperative oxidation of two or three substrates was accompanied with the dramatic increase in the total respiration rates. Our results showed that the alternative (Alt) pathway was more active in malate oxidation at pH 6.8 with CoA and NAD+ where ME operated and was stimulated, indicating that both ME and Alt pathway were related to malate decarboxylation during the light. In K. pinnata mitochondria, NADH and NADPH oxidations were more sensitive with KCN than that with succinate and malate oxidations, suggesting that these oxidations were engaged to cytochrome pathway rather than to Alt pathway and these capacities would be desirable to supply enough energy for cytosol pyruvate orthophosphate dikinase activity.

本文言語英語
ページ(範囲)201-208
ページ数8
ジャーナルBiologia Plantarum
49
2
DOI
出版ステータス出版済み - 6 1 2005
外部発表はい

All Science Journal Classification (ASJC) codes

  • 植物科学
  • 園芸学

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