Terminal oxidases of Chlorella pyrenoidosa

In studies of the kinetics of oxygen uptake by glucose-stimulated Chlorella pyrenoidosa, two terminal oxidases could be distinguished. The cytochrome oxidase of Chlorella has a $\text{K}m(\text{O}_{2})$ of 2.1 ± 0.3 μM, while the second oxidase has a $\text{K}m(\text{O}_{2})$ of 6.7 ± 0.5 μM, and a...

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Veröffentlicht in:Plant physiology (Bethesda) 1972-05, Vol.49 (5), p.775-778
Hauptverfasser: Sargent, D.F, Taylor, C.P.S
Format: Artikel
Sprache:eng
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Zusammenfassung:In studies of the kinetics of oxygen uptake by glucose-stimulated Chlorella pyrenoidosa, two terminal oxidases could be distinguished. The cytochrome oxidase of Chlorella has a $\text{K}m(\text{O}_{2})$ of 2.1 ± 0.3 μM, while the second oxidase has a $\text{K}m(\text{O}_{2})$ of 6.7 ± 0.5 μM, and a maximum capacity about one-quarter of that of the cytochrome system. The identity of the second oxidase is unknown, but it is not inhibited by carbon monoxide, 1 mM cyanide, 0.1 mM thiocyanate, or 1 mM 8-hydroxyquinoline. In fresh cultures, the second oxidase accounts for at most 35% of the total oxygen uptake.
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.49.5.775