Characterization of Mitochondrial NADH Dehydrogenase in Lentinus edodes

표고버섯의 미토콘드리아성 NADH 탈수소효소의 특성

  • Kim, Eun-Mi (Department of Chemistry, Dongguk University) ;
  • Min, Ji-Young (Department of Applied Biology, Dongguk University) ;
  • Min, Tae-Jin (Department of Chemistry, Dongguk University)
  • 김은미 (동국대학교 이과대학 화학과) ;
  • 민지영 (동국대학교 생명자원과학대학 응용생물학과) ;
  • 민태진 (동국대학교 이과대학 화학과)
  • Published : 1998.03.30

Abstract

Mitochondria were isolated from Lentinus edodes and properties of the mitochondrial NADH dehydrogenase were studied. Optimal pH, temperature, and thermal stability of the enzyme were estimated to be 7.6, $33^{\circ}C$, and stable for one hour at $50^{\circ}C$. The apparent $K_m$ for the NADH was 0.33 mM. This enzyme catalyzed to transfer electrons from NADH to ferricyanide, decylubiquinone, and 2,6-dichloro-phenol-indophenol. 0.5 mM antimycin A and 0.01 mM dibromothymoquinone strongly inhibited 87.8% and 76.5% of the enzyme activities. 0.01 mM oligomycin known as an inhibitor of ATPase also strongly inhibited 79.2% of activities. 0.5 mM 5,5'-dithiobis-(2-nitrobenzoic acid) and 1.0 mM N-ethylmaleimide known as a modifier of SH group inhibited 50.4% and 36.7% of activities. 1 mM ethyl 2,4-dihydroxy-6-methyl benzoate and 10 mM orcinol, which had been known as an antibiotics isolated from Umbilicaria vellea according to our previous work, stimulated 68.4% and 48.1% of the enzyme activities.

Keywords

References

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