Terminal Oxidases of Chlorella pyrenoidosa
- 1 May 1972
- journal article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 49 (5), 775-778
- https://doi.org/10.1104/pp.49.5.775
Abstract
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 Km (O(2)) of 2.1 +/- 0.3 mum, while the second oxidase has a Km (O(2)) of 6.7 +/- 0.5 mum, 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.Keywords
This publication has 4 references indexed in Scilit:
- A stable long-term differentiator and its use in the automatic recording of enzyme keneticsAnalytical Biochemistry, 1971
- Specific Inhibition of the Cyanide-insensitive Respiratory Pathway in Plant Mitochondria by Hydroxamic AcidsPlant Physiology, 1971
- Metabolism of Indoleacetic Acid in Rust Diseases. II. Metabolites of Carboxyl-labeled Indoleacetic Acid in TissuesPlant Physiology, 1964
- EFFECTS OF STARVATION ON THE METABOLISM OF CHLORELLAPlant Physiology, 1949