Journal of Life Science (생명과학회지)

Korean Society of Life Science (한국생명과학회)
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Relationship of the Redox State of Pyridine Nucleotides and Quinone Pool with Spectral Complex Formation in Rhodobacter sphaeroides 2.4.1

Rhodobacter sphaeroides 2.4.1 내의 pyridine nucleotide와 quinone pool의 redox 상태와 광합성기구의 합성과의 상관관계

  • 고인정 (KAIST 부설 한국과학영재학교) ;
  • 오정일 (부산대학교 미생물학과)
  • Published : 2009.07.30
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Abstract

The homeostasis of the pyridine nucleotide pool [NAD(P)H and NAD(P)$^+$] is maintained in Rhodobacter sphaeroides mutant strains defective in the cytochrome bci complex or the cytochrome c oxidases in terms of its concentration and redox state. Aerobic derepression of the puf operon, which is under the control of the PrrBA two-component system, in the CBB3 mutant strain of R. sphaeroides was shown to be not the result of changes in the redox state of the pyridine nucleotides and the ubiquinone/ubiquinol pool. Using the bc$_1$ complex knock-out mutant strain of R. sphaeroides, we clearly demonstrated that the inhibitory effect of cbb$_3$, oxidase on spectral complex formation is not caused indirectly by the redox change of the ubiquinone/ubiquinol pool.

호흡전자전달계의 cytochrome bc$_1$ complex 또는 cytochrome c oxidase가 기능을 하지 않는 Rhodobacter sphaeroides mutant 내에서 pyridine nucleotide[NAD(P)H와 NAD(P)$^+$]의 농도와 redox 상태는 wild type과 비교할 때 큰 변화가 없었다. 높은 산소분압 조건에서 키운 Rhodobacter sphaeroides cbb$_3$ oxidase mutant 내에서 PrrBA two-component system에 의해서 조절되는 puf 오페론의 발현은 pyridine nucleotide나 전자전달계의 ubiquinone/ubiquinol pool의 redox 상태의 변화에 의해 유도된 것이 아니다. R. sphaeroides cytochrome bc$_1$ complex mutant를 이용하여 광합성기구 합성에 대한 cbb$_3$ cytochrome c oxidase의 억제 효과는 ubiquinone/ubiquinol pool의 redox 변화에 의해 간접적으로 일어나는 것이 아님을 증명하였다.

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References

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