Rhodopseudomonas gelatinosa의 chromatophore에서 시토크롬 $bc_1$ 복합체와 시토크롬 c 산화효소의 확인 및 특성연구

Identification and characterization of cytochrome $bc_1$ complex and cytochrome c oxidase in chromatophore of rhodopseudomonas gelatinosa

  • 강대길 (전남대학교 자연과학대학 화학과) ;
  • 최명재 (전남대학교 자연과학대학 화학과) ;
  • 최원기 (전남대학교 자연과학대학 화학과)
  • 발행 : 1991.09.01

초록

The chromatophore from the chemotrophically grown facultative anaerobic photosynthetic bacterium, Rhodopseudomonas gelatinosa ATCC 17013 was isolated through stepwise sucrose gradient centrifugation. The isolated chromatophore showed high activities of the cytochrome $bc_{1}$ complex and cytochrome c oxidase. The activity of cytochrome $bc_{1}$ complex was completely inhibited by .5$\mu$M antimycin A,10$\mu$M myxothiazol, and that of cytochrome c oxidase was completely inhibited by .$50\mu$M KCM and $100\mu$M $NaN_{3}$but not inhibited by carbon monoxie. The activity of cytochrome c oxidase of th chromatophore was increased by addition of ionophores or protonophores. The reduced-oxidised difference sspectrum of cytochrome $bc_{1}$ complex isolated by affivity chromatography showed the absorption maxima at 553 nm(shoulder at 547 nm), 520 nm, and 418.5 nm, on the other hand, that of cytochrome c oxidase showed .alpha., .betha. and soret peaks at 554 nm, 523 nm, and 421 nm, respectively. The cytochrome c oxidase from chemotrophically grown Rhodopseudomonas gelatinosa seems to be a b-type cytochrome c oxidase.

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