Autor: |
Stewart, William D.P., Stewart, William D.P., Stewart, William D.P., Stewart, William D.P., Stewart, William D.P. |
Zdroj: |
Israel Journal of Plant Sciences; May 1982, Vol. 31 Issue: 1-4 p168-189, 22p |
Abstrakt: |
The ability of various cyanobacteria (blue-green algae) to fix N2is now well established. The most studied unicellular N2-fixing form is Gloeothece; about half the non-hetero- cystous forms fix N2anaerobically, and heterocystous forms usually fix N2aerobically and anaerobically. Cyanobacterial nitrogenase is little different to that of other N2- fixing prokaryotes, and the enzyme is extremely O2sensitive. This O2sensitivity can be partially overcome by H2; the reductant source for nitrogenase is fixed carbon from the vetative cells and H2utilized by an uptake hydrogenase in heterocysts can also support nitrogenase activity. There is evidence that Φψ may be involved in regulation of nitrogenase activity. ATP can be generated by photophosphorylation and respiration in heterocysts, and the primary route of NH4assimilation is the glutamine synthetase-glutamate synthase pathway. Characteristics of purified glutamine synthetase from heterocystous and non-heterocystous cyanobacteria are presented. Possible interrelations of vegetative cells and heterocysts with respect to N2-fixation are briefly considered. |
Databáze: |
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