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Gene Review:

Synpcc7942_1499 - ferredoxin (2Fe-2S)

Synechococcus elongatus PCC 7942

Hirasawa, M. et al., Bovy, A. et al., Sonoike, K. et al., van der Plas, J. et al.

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Disease relevance of Synpcc7942_1499

Coding sequence of a ferredoxin gene from Anacystis nidulans R2 (Synechococcus PCC7942) [1].
This strategy was based on the observation that the level of the Anabaena ferredoxin mRNA did not increase upon iron addition in Synechococcus [2].

High impact information on Synpcc7942_1499

We have previously reported that the ferredoxin I gene from Synechococcus sp. PCC 7942 is regulated by iron at the level of differential mRNA stability [2].
Addition of the translation inhibitor chloramphenicol to the cultures led to a rapid stabilization, in low- and high-iron conditions, of the wild-type Synechococcus ferredoxin transcript as well as all chimaeric ferredoxin transcripts tested [2].
These results suggest that an electrostatically stabilized complex between Synechococcus nitrate reductase and ferredoxin plays an important role in the mechanism of nitrate reduction catalyzed by this enzyme [3].
Treatment of Synechococcus nitrate reductase with either an arginine-modifying reagent or a lysine-modifying reagent inhibited the ferredoxin-dependent activity of the enzyme but did not affect the methyl viologen-dependent activity [3].
These results suggest that lysine and arginine residues are present at the ferredoxin-binding site of Synechococcus nitrate reductase [3].

Anatomical context of Synpcc7942_1499

Ferredoxin at or below 1 microM can accept electrons from (FA/FB)- effectively competing with the back reaction between P-700+ and (FA/FB)- in the thylakoid membranes and PS I complexes that contained all the eight small subunits [4].

Associations of Synpcc7942_1499 with chemical compounds

When reduced ferredoxin served as the electron donor for the reduction of nitrate to nitrite, the activity of the enzyme declined markedly as the ionic strength increased [3].

References

Coding sequence of a ferredoxin gene from Anacystis nidulans R2 (Synechococcus PCC7942). van der Plas, J., de Groot, R.P., Woortman, M.R., Weisbeek, P.J., van Arkel, G.A. Nucleic Acids Res. (1986) [Pubmed]
Iron-dependent protection of the Synechococcus ferredoxin I transcript against nucleolytic degradation requires cis-regulatory sequences in the 5' part of the messenger RNA. Bovy, A., de Kruif, J., de Vrieze, G., Borrias, M., Weisbeek, P. Plant Mol. Biol. (1993) [Pubmed]
Complex formation between ferredoxin and Synechococcus ferredoxin: nitrate oxidoreductase. Hirasawa, M., Rubio, L.M., Griffin, J.L., Flores, E., Herrero, A., Li, J., Kim, S.K., Hurley, J.K., Tollin, G., Knaff, D.B. Biochim. Biophys. Acta (2004) [Pubmed]
Small subunits of Photosystem I reaction center complexes from Synechococcus elongatus. II. The psaE gene product has a role to promote interaction between the terminal electron acceptor and ferredoxin. Sonoike, K., Hatanaka, H., Katoh, S. Biochim. Biophys. Acta (1993) [Pubmed]

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