1887

Abstract

Cell-free preparations have been made from A2 that are capable of the complete oxidation of thiosulphate to sulphate and of coupling the associated electron transport to ATP synthesis with a P/O ratio of about one. Spectrophotometric measurements and the effect of electron transport chain inhibitors on cytochrome reduction and oxygen uptake indicate that thiosulphate oxidation is coupled directly to cytochrome reduction and does not involve cytochrome . Complete inhibition of phosphorylation by, 2,4-dinitrophenol suggests that ATP synthesis was effected exclusively by electron transport phosphorylation accompanying re-oxidation of cytochrome . Enzymes for thiosulphate oxidation to sulphate and the reduction of cytochrome were located in the supernatant fraction after centrifuging at 130000 , but oxygen uptake required the 130000 pellet fraction, which provided membrane-bound cytochrome c and cytochrome oxidase.

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/content/journal/micro/10.1099/00221287-129-6-1661
1983-06-01
2022-01-25
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