Electron Transport System in the Cell Fraction of the Reiter Treponeme with Special Reference to the Presence of Cytochromes

Abstract

Cells of the Reiter treponeme were disrupted by sonication and fractionated by differential centrifugation. The cell fractions were tested for the electron transport system. The particulate fractions gave a reduced with Na₂S₂O₄ minus oxidized difference spectrum consisting of peaks at 630, 562, 530 and 429mμ. The peaks at 630 and 562mμ seem to correspond to α-bands of a₂-and b-types of cytochromes respectively and the peak at 530mμ may be characteristic of a β-band of the cytochrome b. The high peak at 429mμ may correspond to a Soret band of the cytochrome b. A marked trough with its maximum at 460mμ may be attributed to flavoprotein. Since only the Soret region at 429mμ can scarcely be seen in the supernatant following centrifugation at 104, 000×g, the cytochromes of the treponeme appear to be associated with the cytoplasmic membrane and the membranous structure as in bacterial cells. Higher activity of succinic dehydrogenase was localized in the particulate fractions than the supernatant obtained by centrifugation at 104, 000×g. NADH₂ oxidase activity was found both particulate and supernatant fractions, but was generally higher in the supernatant fraction.