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The role of glutathione and ascorbate in hydroperoxide removal in cyanobacteria.

Authors :
Tel-Or E
Huflejt M
Packer L
Source :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1985 Oct 30; Vol. 132 (2), pp. 533-9.
Publication Year :
1985

Abstract

The antioxidative potential of cyanobacteria to scavenge hydroperoxides formed as by-products of photosynthetic activity was investigated in Nostoc muscorum 7119 and Synechococcus 6311. These cells contained a high concentration of glutathione, 2-5 mM, and a low concentration of ascorbate, 20-100 uM. No glutathione peroxidase was detected while the activity of ascorbate peroxidase was high, reacting with hydrogen peroxide, t-butyl hydroperoxide, and cumene hydroperoxide. Dehydroascorbate reductase was active in recycling ascorbate and glutathione reductase regenerated glutathione from glutathione disulphide. The activity of these antioxidative enzymes in the cyanobacteria was sufficient to remove between 60-230 nmoles H2O2 .mg protein-1 min-1. It is suggested that in cyanobacteria an effective reaction sequence for removal of hydroperoxides involves ascorbate peroxidase and recycling of glutathione and ascorbate.

Details

Language :
English
ISSN :
0006-291X
Volume :
132
Issue :
2
Database :
MEDLINE
Journal :
Biochemical and biophysical research communications
Publication Type :
Academic Journal
Accession number :
3933503
Full Text :
https://doi.org/10.1016/0006-291x(85)91166-0