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Gene Review

petF  -  ferredoxin I

Nostoc sp. PCC 7120

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Disease relevance of petF

  • The Anabaena petF gene is a single-copy gene [1].
  • The gene is transcribed only under anaerobic nitrogenase-inducing conditions, whereas the Plectonema petF gene, encoding a different (type 1) [2Fe-2S] ferredoxin, is only transcribed in cultures growing with combined nitrogen [2].
  • This finding provides a structural basis for explaining the different chemical and functional properties of Nostoc strain MAC ferredoxin II reported in a previous paper (Hutson et al. (1978) Biochem. J. 172, 465-477) [3].
  • Comparing these sequences with those of ferredoxins from Chlorogloeopsis fritschii and Synechocystis 6714, which are also capable of growing under both conditions, showed that Nostoc strain MAC ferredoxin II had unique amino acids around the [2Fe-2S] cluster [3].

High impact information on petF

  • They are part of two different nif gene clusters, nif1 and nif2. fdxH1 encodes the [2Fe-2S] ferredoxin that is known as the direct electron donor to nitrogenase in heterocysts, and is very similar to FdxH from Anabaena sp. PCC 7120 [4].
  • Ferredoxin (Fd) functions in photosynthesis to transfer electrons from photosystem I to ferredoxin-NADP+ reductase (FNR) [5].
  • We have made several site-directed mutants of Anabaena 7120 Fd and have used laser flash photolysis to investigate the effects of these mutations on the kinetics of reduction of oxidized Fd by deazariboflavin semiquinone (dRfH.) and the reduction of oxidized Anabaena FNR by reduced Fd [5].
  • Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin from Anabaena 7120 determined to 1.7-A resolution [6].
  • The [2Fe-2S] ferredoxin produced in the heterocyst cells of Anabaena 7120 plays a key role in nitrogen fixation, where it serves as an electron acceptor from various sources and an electron donor to nitrogenase [6].

Chemical compound and disease context of petF


Biological context of petF

  • The DNA sequence of petF suggests that, in contrast to the nucleus-encoded plant protein, cyanobacterial apoferredoxin is not synthesized as a higher-molecular-weight precursor [1].
  • During growth on complete medium it was transcribed into a monocistronic mRNA species of approximately 500 bases that initiated 100 base pairs upstream from the petF coding region [1].
  • Mixtures of tetradecanucleotides and heptadecanucleotides, each containing all possible DNA sequences corresponding to two separate regions of the ferredoxin amino acid sequence, were synthesized and used as hybridization probes to identify a genomic clone containing the coding sequence for the petF gene [1].
  • The molecular structure of the oxidized form of the [2Fe-2S] ferredoxin isolated from the cyanobacterium Anabaena species strain PCC 7120 has been determined by X-ray diffraction analysis to a nominal resolution of 2.5 A and refined to a crystallographic R factor of 18.7% [7].
  • 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 [2].

Associations of petF with chemical compounds

  • Consequently, a high-resolution X-ray analysis of this [2Fe-2S] ferredoxin, and subsequent three-dimensional comparisons with other known ferredoxin models, will provide new insight into structure/function relationships for this class of redox proteins [9].
  • In contrast to data reported for the spinach system, the stoichiometry of the cross-linked complex between ferredoxin and glutamate synthase was 1:1 [10].

Other interactions of petF

  • The fdxH gene encodes a [2Fe-2S]-type ferredoxin, 98 amino acids in length, with a deduced molecular mass of 10.9 kDa [2].

Analytical, diagnostic and therapeutic context of petF


  1. Isolation and sequence of the gene for ferredoxin I from the cyanobacterium Anabaena sp. strain PCC 7120. Alam, J., Whitaker, R.A., Krogmann, D.W., Curtis, S.E. J. Bacteriol. (1986) [Pubmed]
  2. 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]
  3. Amino acid sequences of Nostoc strain MAC ferredoxins I and II. Hase, T., Matsubara, H., Hutber, G.N., Rogers, L.J. J. Biochem. (1982) [Pubmed]
  4. Distinct and differently regulated Mo-dependent nitrogen-fixing systems evolved for heterocysts and vegetative cells of Anabaena variabilis ATCC 29413: characterization of the fdxH1/2 gene regions as part of the nif1/2 gene clusters. Schrautemeier, B., Neveling, U., Schmitz, S. Mol. Microbiol. (1995) [Pubmed]
  5. Amino acid residues in Anabaena ferredoxin crucial to interaction with ferredoxin-NADP+ reductase: site-directed mutagenesis and laser flash photolysis. Hurley, J.K., Salamon, Z., Meyer, T.E., Fitch, J.C., Cusanovich, M.A., Markley, J.L., Cheng, H., Xia, B., Chae, Y.K., Medina, M. Biochemistry (1993) [Pubmed]
  6. Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin from Anabaena 7120 determined to 1.7-A resolution. Jacobson, B.L., Chae, Y.K., Markley, J.L., Rayment, I., Holden, H.M. Biochemistry (1993) [Pubmed]
  7. Crystallization and structure determination to 2.5-A resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120. Rypniewski, W.R., Breiter, D.R., Benning, M.M., Wesenberg, G., Oh, B.H., Markley, J.L., Rayment, I., Holden, H.M. Biochemistry (1991) [Pubmed]
  8. Multinuclear magnetic resonance studies of the 2Fe.2S* ferredoxin from Anabaena species strain PCC 7120. 2. Sequence-specific carbon-13 and nitrogen-15 resonance assignments of the oxidized form. Oh, B.H., Mooberry, E.S., Markley, J.L. Biochemistry (1990) [Pubmed]
  9. Crystallization and preliminary analysis of oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin from Anabaena 7120. Jacobson, B.L., Chae, Y.K., Böhme, H., Markley, J.L., Holden, H.M. Arch. Biochem. Biophys. (1992) [Pubmed]
  10. 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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