SUMMARY: Ultraviolet spectroscopy, partition chromatography and mass spectroscopy showed that the only quinone isolated from was menaquinone-7. The concentration of quinone present in electron-transport particles was consistent with its participation as an oxido-reduction component. Loss in NADH oxidase activity after ultraviolet irradiation or pentane extraction correlated with the degradation or removal respectively of menaquinone-7 present in the electron transport particles. Attempts to restore NADH oxidase activity either with ultraviolet-treated or pentane-extracted particles using the natural menaquinone were unsuccessful, although lower menaquinone homologues stimulated activity.


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