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

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

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

Abstract

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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