Purification and properties of a flavodoxin from the heterocystous cyanobacterium Anabaena sphaerica.
A flavodoxin was purified to homogeneity from the nitrogen-fixing heterocystous cyanobacterium Anabaena sphaerica grown under iron-limited conditions. The protein has a molecular mass of 21 kDa, and its spectral properties and amino-acid composition are very close to that of flavodoxins from other cyanobacteria. A. sphaerica flavodoxin supported the activities of A. sphaerica NADP reductase and Clostridium butyricum hydrogenase in reconstituted systems with illuminated plant chloroplasts as reductant. With the use of polyclonal anti-flavodoxin antiserum it was found that nitrogen-fixing cultures of A. sphaerica grown under iron-sufficient conditions contain low but significant amounts of flavodoxin (0.2-0.6 micrograms/mg crude extract protein) which increased dramatically (to 8-15 micrograms/mg crude extract protein) after the iron concentration in the medium was decreased to below 1 microM Fe. The flavodoxin content of both iron-limited and iron-sufficient. A. sphaerica was also shown to depend upon the growth phase of the (batch) cultures with a maximum at early exponential phase, coinciding with maximal in-vivo nitrogenase activity. These results suggest that A. sphaerica flavodoxin not only substitutes for ferredoxin under iron-limiting conditions, but also fulfills some specific role under iron-sufficient conditions.
Yakunin
A F
AF
Institute of Soil Science and Photosynthesis, Pushchino, Moscow region, Russia.
Hallenbeck
P C
PC
Troshina OYu
Gogotov
I N
IN
D000596:Amino Acids / Q000032:analysis; D017033:Anabaena / Q000378:metabolism*; D004579:Electron Transport; D005287:Ferredoxin-NADP Reductase / Q000378:metabolism; D005418:Flavodoxin / Q000096:biosynthesis / Q000302:isolation & purification*; D009586:Nitrogen Fixation
D000596:Amino Acids; D005418:Flavodoxin; D005287:Ferredoxin-NADP Reductase