Electron donation to nitrogenase in heterocysts of cyanobacteria
β Scribed by Gabriele Neuer; Hermann Bothe
- Book ID
- 104762842
- Publisher
- Springer
- Year
- 1985
- Tongue
- English
- Weight
- 767 KB
- Volume
- 143
- Category
- Article
- ISSN
- 0302-8933
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β¦ Synopsis
Various electron donors were found to stimulate C2H2 reduction (N2 fixation) by isolated heterocysts from Anabaena variabilis and Anabaena cylindrica. Intermediates of glycolysis and the tricarboxylic acid cycle as well as unphosphorylated sugars like glucose, fructose and erythrose were among these electron donors. The transfer of electrons from donors like Hz, NADH, glyoxylate and glycollate was strictly light-dependent, whereas others like NADPH or pyruvate plus coenzyme A supported C2H2 reduction also in the dark. In all cases, the overall activity was enhanced by light. The stimulation by light was more distinct with heterocysts from A. variabilis than with heterocysts from A. cylindrica.
The present communication establishes that pyruvate supports C2H2 reduction by heterocysts from either A. variabilis or A. cylindrica with rates comparable to those with other electron donors. Pyruvate could, however, support C2H2 reduction only in the presence of coenzyme A, and the concentrations of both coenzyme A and pyruvate were crucial. A pyruvate-dependent reduction of ferredoxin by extracts from heterocysts was recorded spectrophotometrically. Glyoxylate, which is an inhibitor of thiamine pyrophosphate-dependent decarboxylations, inhibited pyruvate-dependent C2H2 reduction. This result supports the conclusion that pyruvate is metabolised by pyruvate: ferredoxin oxidoreductase in heterocysts. High concentrations of pyruvate and other electron donors inhibited C2Hz reduction which suggests that nitrogenase activity in heterocysts may be controlled by the availability of electron donors.
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