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Gene Review

DVU2797  -  ferredoxin

Desulfovibrio vulgaris str. Hildenborough

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Disease relevance of DVU2797

  • Orf6 is a cytoplasmic redox protein containing two iron-sulfur clusters, as indicated by its similarity to the ferredoxin domain of [Fe] hydrogenase from Desulfovibrio species [1].

High impact information on DVU2797

  • Although the genome annotation implicates a ferredoxin-dependent oxoglutarate synthase, isotopic evidence does not support flux through this reaction in either the oxidative or the reductive mode; therefore, the TCA cycle is incomplete [2].
  • The periplasmic Fe-hydrogenase from Desulfovibrio vulgaris (Hildenborough) contains three iron-sulfur prosthetic groups: two putative electron transferring [4Fe-4S] ferredoxin-like cubanes (two F-clusters), and one putative Fe/S supercluster redox catalyst (one H-cluster) [3].

Associations of DVU2797 with chemical compounds

  • These results, therefore, suggest that two electron-transferring ferredoxin-like [4Fe-4S] clusters are located in the NH2-terminal segment of the hydrogenase molecule [4].


  1. The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough encodes a potential transmembrane redox protein complex. Rossi, M., Pollock, W.B., Reij, M.W., Keon, R.G., Fu, R., Voordouw, G. J. Bacteriol. (1993) [Pubmed]
  2. Pathway confirmation and flux analysis of central metabolic pathways in Desulfovibrio vulgaris hildenborough using gas chromatography-mass spectrometry and Fourier transform-ion cyclotron resonance mass spectrometry. Tang, Y., Pingitore, F., Mukhopadhyay, A., Phan, R., Hazen, T.C., Keasling, J.D. J. Bacteriol. (2007) [Pubmed]
  3. Redox properties of the iron-sulfur clusters in activated Fe-hydrogenase from Desulfovibrio vulgaris (Hildenborough). Pierik, A.J., Hagen, W.R., Redeker, J.S., Wolbert, R.B., Boersma, M., Verhagen, M.F., Grande, H.J., Veeger, C., Mutsaers, P.H., Sands, R.H. Eur. J. Biochem. (1992) [Pubmed]
  4. Nucleotide sequence of the gene encoding the hydrogenase from Desulfovibrio vulgaris (Hildenborough). Voordouw, G., Brenner, S. Eur. J. Biochem. (1985) [Pubmed]
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