Role of calcium in the inhibition of nitrogenase activity by Methylparathion and Benthiocarb in the cyanobacteriumNostoc muscorum
β Scribed by A. K. Bhunia; N. K. Basu; D. Roy; S. K. Banerjee
- Publisher
- Springer
- Year
- 1994
- Tongue
- English
- Weight
- 321 KB
- Volume
- 10
- Category
- Article
- ISSN
- 1573-0972
No coin nor oath required. For personal study only.
β¦ Synopsis
Methylparathion and Benthiocarb inhibition of N2 fixation in the cyanobacterium Nostoc muscorum was reversed by Ca(2+) at 1 mM but not at 0.1 mM. The concentration of intracellular Ca(2+) was relatively high in the presence of these pesticides when 1 mM Ca(2+) was also present, indicating that intracellular Ca(2+) may participate in protecting nitrogenase activity against Methylparathion and Benthiocarb.
π SIMILAR VOLUMES
Ammonium at 5mM completely inhibited nitrogenase activity of Nostoc ANTH but only slightly inhibited the membrane potential, indicating that these two events are independent and that nitrogenase activity is not regulated by the latter.
## Abstract Growth and urea regulation of heterocyst and nitrogenase formation have been studied in the diazotrophic cyanobacterium __Anabaena cycadeae__ and its glutamine auxotrophic mutant strain lacking glutamine synthetase (GS) activity. The parent strain having normal GS activity utilized urea
## Abstract Oxygenβdependent regulation of HIFβ1 activity occurs at multiple levels in vivo. The mechanisms regulating HIFβ1Ξ± protein expression have been most extensively analyzed but the ones modulating HIFβ1 transcriptional activity remain unclear. Changes in the phosphorylation and/or redox sta