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dc.contributor.authorHickey, Christopher W.
dc.contributor.authorDaniel, Roy M.
dc.date.accessioned2010-09-02T02:41:19Z
dc.date.available2010-09-02T02:41:19Z
dc.date.issued1979
dc.identifier.citationHickey, C.W. & Daniel, R.M. (1979). The electron transport system of an extremely thermophilic bacterium. Journal of General Microbiology, 114(1), 195-200.en_NZ
dc.identifier.urihttps://hdl.handle.net/10289/4512
dc.description.abstractActive, membrane-bound NADH and succinate oxidase activities with a temperature optimum of 75 ℃ were demonstrated in an extremely thermophilic bacterium. These were relatively stable in cell-free extracts and respiratory particles at 75 ℃, but at 90 ℃ the half-lives of these oxidase systems were about 15 min in respiratory particles and 80 min in cell-free extracts. The stability of the NADH oxidase in respiratory particles at 90 ℃ was enhanced by 2 M-(NH₄)₂SO₄, 50% (v/v) glycerol and by NADH. A number of other substrates were oxidized by the electron transport system. Respiratory particles contained cytochromes a-613, a-602, b-559, cytochrome o and at least one c-type cytochrome, c-555. The soluble fraction contained at least two c-type cytochromes, at least one of which was CO-reactive. The sensitivity of NADH and succinate oxidases to a range of inhibitors was determined.en_NZ
dc.language.isoen
dc.subjectbiologyen_NZ
dc.titleThe electron transport system of an extremely thermophilic bacteriumen_NZ
dc.typeJournal Articleen_NZ
dc.identifier.doi10.1099/00221287-114-1-195en_NZ


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