Glutathione reductase activity was detected and characterized in heterocysts and vegetative cells of the cyanobacterium Nostoc muscorum. The activity of the enzyme varied between 50 and 150 nmol reduced glutathione· min-1·mg protein-1, and the apparent Km for NADPH was 0.125 and 0.200 mM for heterocysts and vegetative cells, respectively. The enzyme was found to be sensitive to Zn+2 ions, however, preincubation with oxidized glutathione rendered its resistance to Zn+2 inhibition. Nostoc muscorum filaments were found to contain 0.6–0.7mM glutathione, and it is suggested that glutathione reductase can regenerate reduced glutathione in both cell types. The combined activity of glutathione reductase and isocitrate dehydrogenase in heterocysts was as high as 18 nmol reduced glutathione·min-1·mg protein-1. A relatively high superoxide dismutase activity was found in the two cell types; 34.2 and 64.3 enzyme units·min-1·mg protein-1 in heterocysts and vegetative cells, respectively.
We suggest that glutathione reductase plays a role in the protection mechanism which removes oxygen radicals in the N2-fixing cyanobacterium Nostoc muscorum.
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Similar content being viewed by others Explore related subjectsDiscover the latest articles and news from researchers in related subjects, suggested using machine learning. Abbreviations5-5′-dithiobis-(2-nitrobenzoic acid)
ethylenediaminetetra-acetic acid
glutathione reductase (EC1.6.4.2)
reduced glutathione
oxidized glutathione
O-phtaldialdehyde
superoxide dismutase (EC 1.15.1.1)
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Department of Agricultural Botany, Faculty of Agriculture, The Hebrew University of Jerusalem, P.O. Box 12, 76100, Rehovot, Israel
Leah Karni, Stephen J. Moss & Elisha Tel-Or
Karni, L., Moss, S.J. & Tel-Or, E. Glutathione reductase activity in heterocysts and vegetative cells of the cyanobacterium Nostoc muscorum . Arch. Microbiol. 140, 215–217 (1984). https://doi.org/10.1007/BF00454930
Received: 26 January 1984
Accepted: 27 July 1984
Issue Date: December 1984
DOI: https://doi.org/10.1007/BF00454930
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