6533b81ffe1ef96bd1277b4a
RESEARCH PRODUCT
Isolation and partial characterization of a cytochrome-o complex from chromatophores of the photosynthetic bacterium Rhodospirillum rubrum FR1.
Klaus DoseThomas NawrothAndré Schrattenholzsubject
Gel electrophoresisOxidase testUbiquinolHemeproteinCytochromebiologyMolecular massChemistryProtein subunitEscherichia coli ProteinsRhodospirillum rubrumPhotosynthetic Reaction Center Complex ProteinsDithioniteBacterial Chromatophoresbiology.organism_classificationCytochrome b GroupBiochemistrychemistry.chemical_compoundBiochemistryBacterial Proteinsbiology.proteinCytochromesElectrophoresis Polyacrylamide GelRhodospirillumdescription
A cytochrome-o complex was isolated from chromatophores of photoheterotrophically grown Rhodospirillum rubrum FR1. The enzyme was extracted with the non-denaturating detergent taurodeoxycholate and subsequently purified by sucrose-density-gradient centrifugation and gel-permeation HPLC. The complex contains two types of cytochromes, one of them cytochrome o, and two copper atoms. It catalyzes the reduction of molecular oxygen, when N,N,N',N'-tetramethyl-p-phenylenediamine or ubiquinol 10 are offered as electron donors. The oxidase activity is inhibited by cyanide, carbon monoxide and 2-heptyl-2-hydroxyquinoline N-oxide. The molecular mass of the protein is 136 +/- 15 kDa. The subunit analysis, by SDS continuous and gradient gels, revealed four subunits with molecular mass 66 kDa (subunit I), 36 kDa (subunit II), 20 kDa (subunit III) and 11 kDa (subunit IV).
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1989-05-01 | European journal of biochemistry |