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Gene Review

fixX  -  ferredoxin-like protein

Escherichia coli CFT073

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Disease relevance of fixX


High impact information on fixX

  • The enzyme contains four ferredoxin-like Cys groups in the electron transfer subunit, DmsB, and an additional group of Cys residues in the catalytic subunit, DmsA [3].
  • The results show the reduction potentials in the midrange for ferredoxin-like [4Fe-4S] clusters [4].
  • This protein is designated as PFLP (plant ferredoxin-like protein) by virtue of its high homology with plant ferredoxin protein containing an N-terminal signal peptide responsible for chloroplast targeting and a putative 2Fe-2S domain responsible for redox activity [5].
  • The reductase partner comprises flavin mononucleotide- and NADH-binding motifs and a [2Fe2S] ferredoxin-like center [6].
  • The deduced human ETF-QO sequence predicts a protein containing 617 amino acids (67 kDa), two domains associated with the binding of the AMP moiety of the FAD prosthetic group, two membrane helices and a motif containing four cysteine residues that is frequently associated with the liganding of ferredoxin-like iron-sulfur clusters [7].

Biological context of fixX

  • In contrast, ferredoxin-like proteins, which are encoded by nifB-associated genes, are not required for nitrogen fixation in all other organisms analysed so far [8].

Associations of fixX with chemical compounds

  • The 12 cysteine residues present in FrdB form 3 ferredoxin-like clusters, whereas the 12 cysteines of FrdA are not clustered [9].
  • We report here a simple system for the functional expression of various P450 genes using the reductase domain of this P450RhF, which comprises flavin mononucleotide- and nicotinamide adenine dinucleotide phosphate binding motifs and a [2Fe2S] ferredoxin-like center [10].


  1. Second gene (nifH*) coding for a nitrogenase iron protein in Azotobacter chroococcum is adjacent to a gene coding for a ferredoxin-like protein. Robson, R., Woodley, P., Jones, R. EMBO J. (1986) [Pubmed]
  2. Synthesis of the ferredoxin-like protein FdxN from Rhizobium meliloti bacteroids as a fusion protein in Escherichia coli. Riedel, K.U., Masepohl, B., Klipp, W., Pühler, A. Can. J. Microbiol. (1992) [Pubmed]
  3. Engineering a novel iron-sulfur cluster into the catalytic subunit of Escherichia coli dimethyl-sulfoxide reductase. Trieber, C.A., Rothery, R.A., Weiner, J.H. J. Biol. Chem. (1996) [Pubmed]
  4. Cofactor dependence of reduction potentials for [4Fe-4S]2+/1+ in lysine 2,3-aminomutase. Hinckley, G.T., Frey, P.A. Biochemistry (2006) [Pubmed]
  5. Ferredoxin from sweet pepper (Capsicum annuum L.) intensifying harpin(pss)-mediated hypersensitive response shows an enhanced production of active oxygen species (AOS). Dayakar, B.V., Lin, H.J., Chen, C.H., Ger, M.J., Lee, B.H., Pai, C.H., Chow, D., Huang, H.E., Hwang, S.Y., Chung, M.C., Feng, T.Y. Plant Mol. Biol. (2003) [Pubmed]
  6. Identification of a new class of cytochrome P450 from a Rhodococcus sp. Roberts, G.A., Grogan, G., Greter, A., Flitsch, S.L., Turner, N.J. J. Bacteriol. (2002) [Pubmed]
  7. Molecular cloning and expression of a cDNA encoding human electron transfer flavoprotein-ubiquinone oxidoreductase. Goodman, S.I., Axtell, K.M., Bindoff, L.A., Beard, S.E., Gill, R.E., Frerman, F.E. Eur. J. Biochem. (1994) [Pubmed]
  8. The Rhizobium meliloti fdxN gene encoding a ferredoxin-like protein is necessary for nitrogen fixation and is cotranscribed with nifA and nifB. Klipp, W., Reiländer, H., Schlüter, A., Krey, R., Pühler, A. Mol. Gen. Genet. (1989) [Pubmed]
  9. The fumarate reductase operon of Wolinella succinogenes. Sequence and expression of the frdA and frdB genes. Lauterbach, F., Körtner, C., Albracht, S.P., Unden, G., Kröger, A. Arch. Microbiol. (1990) [Pubmed]
  10. Functional expression system for cytochrome P450 genes using the reductase domain of self-sufficient P450RhF from Rhodococcus sp. NCIMB 9784. Nodate, M., Kubota, M., Misawa, N. Appl. Microbiol. Biotechnol. (2006) [Pubmed]
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