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Gene Review

fdxH  -  heterocyst ferredoxin

Nostoc sp. PCC 7120

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Disease relevance of fdxH

  • Southern hybridization detected only one copy of the fdxH gene in the Anabaena 7120 genome [1].
  • To identify amino acids that are important for interaction with nitrogenase, we generated site-directed mutations in the fdxH gene and assayed the in vitro activity of the resulting recombinant proteins isolated from Escherichia coli [2].
  • A genomic DNA region with four consecutive open reading frames, including an fdxH-type gene, has been sequenced and initially characterized for the nonheterocystous nitrogen-fixing cyanobacterium Plectonema boryanum PCC 73110 [3].
  • An fdxB-type gene encoding a 2[4Fe-4S] ferredoxin not previously identified in cyanobacteria is located immediately downstream of fdxH in P. boryanum [3].
  • Genes homologous to ORF3 from the fdxH gene regions of A. variabilis and Plectonema boryanum, the mop genes of Clostridium pasteurianum encoding molybdo-pterin binding proteins, and ORF3 from the A. variabilis hydrogenase gene cluster were identified within the sequenced region [4].

High impact information on fdxH


Chemical compound and disease context of fdxH


Biological context of fdxH


Associations of fdxH with chemical compounds

  • Exchange of residue F65 for aliphatic substitutions, which was crucial to electron transfer to ferredoxin:NADP-reductase and nitrite reductase, exhibited only small effects on glutamate synthase-dependent activity while heterocyst ferredoxin and flavodoxin were almost inactive as electron donors [8].

Other interactions of fdxH

  • The fdxH gene encodes a [2Fe-2S]-type ferredoxin, 98 amino acids in length, with a deduced molecular mass of 10.9 kDa [3].
  • Iron concentrations (1 microM Fe) sufficient to induce synthesis of the vegetative cell flavodoxin did not stimulate diazotrophic growth of the fdxH mutant strains, suggesting that FdxH was not replaced by a NifJ-flavodoxin system [4].


  1. Molecular cloning and nucleotide sequence analysis of the gene coding for heterocyst ferredoxin from the cyanobacterium Anabaena sp. strain PCC 7120. Böhme, H., Haselkorn, R. Mol. Gen. Genet. (1988) [Pubmed]
  2. Evidence from directed mutagenesis that positively charged amino acids are necessary for interaction of nitrogenase with the [2Fe-2S] heterocyst ferredoxin (FdxH) from the cyanobacterium Anabaena sp., PCC7120. Schmitz, S., Schrautemeier, B., Böhme, H. Mol. Gen. Genet. (1993) [Pubmed]
  3. Characterization of the genome region encoding an fdxH-type ferredoxin and a new 2[4Fe-4S] ferredoxin from the nonheterocystous, nitrogen-fixing cyanobacterium Plectonema boryanum PCC 73110. Schrautemeier, B., Cassing, A., Böhme, H. J. Bacteriol. (1994) [Pubmed]
  4. The heterocyst-specific fdxH gene product of the cyanobacterium Anabaena sp. PCC 7120 is important but not essential for nitrogen fixation. Masepohl, B., Schölisch, K., Görlitz, K., Kutzki, C., Bohme, H. Mol. Gen. Genet. (1997) [Pubmed]
  5. Analysis of the hyperfine-shifted nitrogen-15 resonances of the oxidized form of Anabaena 7120 heterocyst ferredoxin. Chae, Y.K., Markley, J.L. Biochemistry (1995) [Pubmed]
  6. Mutations of surface residues in Anabaena vegetative and heterocyst ferredoxin that affect thermodynamic stability as determined by guanidine hydrochloride denaturation. Hurley, J.K., Caffrey, M.S., Markley, J.L., Cheng, H., Xia, B., Chae, Y.K., Holden, H.M., Tollin, G. Protein Sci. (1995) [Pubmed]
  7. Transcriptional and translational analysis of ferredoxin and flavodoxin under iron and nitrogen stress in Anabaena sp. strain PCC 7120. Razquin, P., Schmitz, S., Fillat, M.F., Peleato, M.L., Böhme, H. J. Bacteriol. (1994) [Pubmed]
  8. Glutamate 94 of [2Fe-2S]-ferredoxins is important for efficient electron transfer in the 1:1 complex formed with ferredoxin-glutamate synthase (GltS) from Synechocystis sp. PCC 6803. Schmitz, S., Navarro, F., Kutzki, C.K., Florencio, F.J., Böhme, H. Biochim. Biophys. Acta (1996) [Pubmed]
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