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Gene Review

PF1909  -  ferredoxin

Pyrococcus furiosus DSM 3638

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Disease relevance of PF1909

  • The gene for ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus was cloned, sequenced, and expressed in Escherichia coli [1].
  • Sequence, assembly and evolution of a primordial ferredoxin from Thermotoga maritima [2].
  • In the present study, protein film voltammetry has been used to induce and monitor the oxidative conversion of [4Fe-4S] into [3Fe-4S] clusters in different variants of Azotobacter vinelandii ferredoxin I (AvFdI; the 8Fe form of the native protein), and DeltaThr(14)/DeltaAsp(15), Thr(14)-->Cys (T14C) and C42D mutants [3].
  • The reduced ferredoxin also functioned as an electron donor for H2 evolution catalyzed by the hydrogenase of the mesophilic eubacterium Clostridium pasteurianum [4].

High impact information on PF1909


Chemical compound and disease context of PF1909

  • T. maritima ferredoxin expressed in E. coli is a heat-stable, monomeric protein, the spectroscopic properties of which show that its 4Fe-4S cluster is correctly assembled within the mesophilic host, and that it remains stable during purification under aerobic conditions [2].

Biological context of PF1909


Anatomical context of PF1909

  • Neither highly washed membranes nor the purified enzyme used NAD(P)(H) or P. furiosus ferredoxin as an electron carrier, nor did either catalyze the reduction of elemental sulfur with H(2) as the electron donor [12].

Associations of PF1909 with chemical compounds


Other interactions of PF1909

  • P. furiosus rubredoxin (K(m) = 1.6 microM) also functioned as an electron acceptor for SuDH, and SuDH catalyzed the reduction of NADP with reduced P. furiosus ferredoxin (K(m) = 0.7 microM) as an electron donor [16].

Analytical, diagnostic and therapeutic context of PF1909


  1. Cloning, expression, and molecular characterization of the gene encoding an extremely thermostable [4Fe-4S] ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus. Heltzel, A., Smith, E.T., Zhou, Z.H., Blamey, J.M., Adams, M.W. J. Bacteriol. (1994) [Pubmed]
  2. Sequence, assembly and evolution of a primordial ferredoxin from Thermotoga maritima. Darimont, B., Sterner, R. EMBO J. (1994) [Pubmed]
  3. Influence of electrochemical properties in determining the sensitivity of [4Fe-4S] clusters in proteins to oxidative damage. Tilley, G.J., Camba, R., Burgess, B.K., Armstrong, F.A. Biochem. J. (2001) [Pubmed]
  4. A novel and remarkably thermostable ferredoxin from the hyperthermophilic archaebacterium Pyrococcus furiosus. Aono, S., Bryant, F.O., Adams, M.W. J. Bacteriol. (1989) [Pubmed]
  5. A simple energy-conserving system: proton reduction coupled to proton translocation. Sapra, R., Bagramyan, K., Adams, M.W. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  6. Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase. Ma, K., Hutchins, A., Sung, S.J., Adams, M.W. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  7. The ferredoxin-dependent conversion of glyceraldehyde-3-phosphate in the hyperthermophilic archaeon Pyrococcus furiosus represents a novel site of glycolytic regulation. van der Oost, J., Schut, G., Kengen, S.W., Hagen, W.R., Thomm, M., de Vos, W.M. J. Biol. Chem. (1998) [Pubmed]
  8. Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences. Maeder, D.L., Weiss, R.B., Dunn, D.M., Cherry, J.L., González, J.M., DiRuggiero, J., Robb, F.T. Genetics (1999) [Pubmed]
  9. Spectroscopic characterization of the novel iron-sulfur cluster in Pyrococcus furiosus ferredoxin. Conover, R.C., Kowal, A.T., Fu, W.G., Park, J.B., Aono, S., Adams, M.W., Johnson, M.K. J. Biol. Chem. (1990) [Pubmed]
  10. Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus: the 1.85 A resolution crystal structure and its mechanistic implications. Hu, Y., Faham, S., Roy, R., Adams, M.W., Rees, D.C. J. Mol. Biol. (1999) [Pubmed]
  11. Secondary structure extensions in Pyrococcus furiosus ferredoxin destabilize the disulfide bond relative to that in other hyperthermostable ferredoxins. Global consequences for the disulfide orientational heterogeneity. Wang, P.L., Calzolai, L., Bren, K.L., Teng, Q., Jenney, F.E., Brereton, P.S., Howard, J.B., Adams, M.W., La Mar, G.N. Biochemistry (1999) [Pubmed]
  12. Purification and characterization of a membrane-bound hydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus. Sapra, R., Verhagen, M.F., Adams, M.W. J. Bacteriol. (2000) [Pubmed]
  13. Indolepyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. A new enzyme involved in peptide fermentation. Mai, X., Adams, M.W. J. Biol. Chem. (1994) [Pubmed]
  14. Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus. Mukund, S., Adams, M.W. J. Biol. Chem. (1995) [Pubmed]
  15. A gallium-substituted cubane-type cluster in Pyrococcus furiosus ferredoxin. Johnson, K.A., Brereton, P.S., Verhagen, M.F., Calzolai, L., La Mar, G.N., Adams, M.W., Amster, I.J. J. Am. Chem. Soc. (2001) [Pubmed]
  16. Sulfide dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur. Ma, K., Adams, M.W. J. Bacteriol. (1994) [Pubmed]
  17. Participation of the disulfide bridge in the redox cycle of the ferredoxin from the hyperthermophile Pyrococcus furiosus: 1H nuclear magnetic resonance time resolution of the four redox states at ambient temperature. Gorst, C.M., Zhou, Z.H., Ma, K., Teng, Q., Howard, J.B., Adams, M.W., La Mar, G.N. Biochemistry (1995) [Pubmed]
  18. A pure S = 3/2 [Fe4S4]+ cluster in the A33Y variant of Pyrococcus furiosus ferredoxin. Duderstadt, R.E., Brereton, P.S., Adams, M.W., Johnson, M.K. FEBS Lett. (1999) [Pubmed]
  19. Catalytic properties, molecular composition and sequence alignments of pyruvate: ferredoxin oxidoreductase from the methanogenic archaeon Methanosarcina barkeri (strain Fusaro). Bock, A.K., Kunow, J., Glasemacher, J., Schönheit, P. Eur. J. Biochem. (1996) [Pubmed]
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