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Gene Review

cyf  -  cytochrome c-553

Desulfovibrio vulgaris str. Hildenborough

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Disease relevance of cyf


High impact information on cyf

  • The loss of the hydrogen bond from tyrosine 64 and the increase of the solvent exposure of the heme are probably responsible of the loss of electron transfer between formate dehydrogenase and cytochrome c553 [3].
  • Replacement of tyrosine 64 by alanine in cytochrome c553 from Desulfovibrio vulgarisHildenborough prevents electron transfer with the formate dehydrogenase [3].
  • Unfolding of oxidized and reduced cytochrome c553 by guanidine hydrochloride (GuHCl) was monitored by circular dichroism (CD) and Soret absorption; the same unfolding curves were obtained with both methods supporting that cytochrome c553 unfolds by an apparent two-state process [4].
  • For complexes between flavodoxin and cytochrome c553 this was not the case and a lower correlation was observed between electron tunnelling coupling factors and excess energies [5].
  • The gene sequence indicates cytochrome c553 to be synthesized as a precursor protein with an NH2-terminal signal sequence of 24 residues [6].

Chemical compound and disease context of cyf


Associations of cyf with chemical compounds


Other interactions of cyf


Analytical, diagnostic and therapeutic context of cyf


  1. Overexpression of Desulfovibrio vulgaris Hildenborough cytochrome c553 in Desulfovibrio desulfuricans G200. Evidence of conformational heterogeneity in the oxidized protein by NMR. Blanchard, L., Marion, D., Pollock, B., Voordouw, G., Wall, J., Bruschi, M., Guerlesquin, F. Eur. J. Biochem. (1993) [Pubmed]
  2. Aerobic expression of the cyf gene encoding cytochrome c-553 from Desulfovibrio vulgaris Hildenborough in Escherichia coli. Pollock, W.B., Voordouw, G. Microbiology (Reading, Engl.) (1994) [Pubmed]
  3. Tyrosine 64 of cytochrome c553 is required for electron exchange with formate dehydrogenase in Desulfovibrio vulgaris Hildenborough. Sebban-Kreuzer, C., Blackledge, M., Dolla, A., Marion, D., Guerlesquin, F. Biochemistry (1998) [Pubmed]
  4. Equilibrium unfolding of a small low-potential cytochrome, cytochrome c553 from Desulfovibrio vulgaris. Wittung-Stafshede, P. Protein Sci. (1999) [Pubmed]
  5. Effects of protein-protein interactions on electron transfer: docking and electron transfer calculations for complexes between flavodoxin and c-type cytochromes. Cunha, C.A., Romão, M.J., Sadeghi, S.J., Valetti, F., Gilardi, G., Soares, C.M. J. Biol. Inorg. Chem. (1999) [Pubmed]
  6. Cloning and sequencing of the gene encoding cytochrome c553 from Desulfovibrio vulgaris Hildenborough. van Rooijen, G.J., Bruschi, M., Voordouw, G. J. Bacteriol. (1989) [Pubmed]
  7. 1H-NMR study of the structural influence of Y64 substitution in Desulfovibrio vulgaris Hildenborough cytochrome c553. Sebban-Kreuzer, C., Blanchard, L., Bersch, B., Blackledge, M.J., Marion, D., Dolla, A., Guerlesquin, F. Eur. J. Biochem. (1998) [Pubmed]
  8. Effects of the Tyr64 substitution on the stability of cytochrome c553, a low oxidoreduction-potential cytochrome from Desulfovibrio vulgaris Hildenborough. Blanchard, L., Dolla, A., Bersch, B., Forest, E., Bianco, P., Wall, J., Marion, D., Guerlesquin, F. Eur. J. Biochem. (1994) [Pubmed]
  9. Cytochrome c553 from Desulfovibrio vulgaris (Hildenborough). Electrochemical properties and electron transfer with hydrogenase. Verhagen, M.F., Wolbert, R.B., Hagen, W.R. Eur. J. Biochem. (1994) [Pubmed]
  10. The formate dehydrogenase-cytochrome c553 complex from Desulfovibrio vulgaris Hildenborough. Sebban-Kreuzer, C., Dolla, A., Guerlesquin, F. Eur. J. Biochem. (1998) [Pubmed]
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