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Gene Review

PF1281  -  superoxide reductase

Pyrococcus furiosus DSM 3638

 
 
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Disease relevance of PF1281

  • Redox-dependent structural changes in the superoxide reductase from Desulfoarculus baarsii and Treponema pallidum: a FTIR study [1].
  • The electronic and vibrational properties of the [Fe(His)(4)(Cys)] site (Center II) responsible for catalysis of superoxide reduction in the two-iron superoxide reductase (2Fe-SOR) from Desulfovibrio vulgaris have been investigated using the combination of EPR, resonance Raman, UV/visible/near-IR absorption, CD, and VTMCD spectroscopies [2].
 

High impact information on PF1281

  • Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase [3].
  • The results support a catalytic mechanism for SOR, with the first step involving oxidative addition of superoxide to form a ferric-peroxo intermediate, and indicate the important roles that the Fe spin state and the trans cysteinate ligand play in effecting superoxide reduction and peroxide release [3].
  • In the reduced state, the ferrous site of SOR is shown to have square-pyramidal coordination geometry in frozen solution with four equatorial histidines and one axial cysteine on the basis of XAS and UV and NIR VTMCD studies [4].
  • Resonance Raman and ENDOR studies of SOR variants, in which the conserved glutamate and lysine residues in a flexible loop above the substrate binding pocket have been individually replaced by alanine, indicate that the side chains of these two residues are not involved in direct interaction with bound cyanide [5].
  • Analysis of the 13C hyperfine tensors for the three substates of the 2Fe-SOR within a simple heuristic model for the Fe-C bonding gives values for the Fe-C-N angles in the three substates of ca. 123 degrees (C3) and 133 degrees (C2), taking a reference value from vibrational studies of 175 degrees (C1 species) [5].
 

Biological context of PF1281

  • The archaeal SOR provides a novel mechanism to reduce superoxide and demonstrates the potential for using archaeal genes to alter eukaryotic metabolism [6].
 

Anatomical context of PF1281

  • When produced as a fusion protein with the green fluorescent protein in plant cells, P. furiosus SOR is located in the cytosol and nucleus [6].
 

Associations of PF1281 with chemical compounds

  • The structural and electronic properties of the SOR active site are discussed in relation to the role and bonding of the axial cysteine residue and the recent proposals for the catalytic mechanism [4].
  • To further investigate this non-heme peroxo-iron species, we have carried out a Mössbauer study of the (57)Fe-enriched E47A SOR from D. baarsii reacted quickly with H(2)O(2) [7].
  • The participation of a glutamate as the sixth ligand of some of the iron centres in Pyrococcus furiosus SOR was not observed in TpSOR [8].
  • This is the first demonstration of in vitro superoxide reduction to hydrogen peroxide using NAD(P)H as the electron donor in an SOR-mediated pathway [9].
 

Analytical, diagnostic and therapeutic context of PF1281

  • We have added cyanide to oxidized 1Fe and 2Fe superoxide reductase (SOR) as a surrogate for the putative ferric-(hydro)peroxo intermediate in the reaction of the enzymes with superoxide and have used vibrational and ENDOR spectroscopies to study the properties of the active site paramagnetic iron center [5].

References

  1. Redox-dependent structural changes in the superoxide reductase from Desulfoarculus baarsii and Treponema pallidum: a FTIR study. Berthomieu, C., Dupeyrat, F., Fontecave, M., Verméglio, A., Nivière, V. Biochemistry (2002) [Pubmed]
  2. Spectroscopic characterization of the [Fe(His)(4)(Cys)] site in 2Fe-superoxide reductase from Desulfovibrio vulgaris. Clay, M.D., Emerson, J.P., Coulter, E.D., Kurtz, D.M., Johnson, M.K. J. Biol. Inorg. Chem. (2003) [Pubmed]
  3. Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase. Clay, M.D., Cosper, C.A., Jenney, F.E., Adams, M.W., Johnson, M.K. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  4. Spectroscopic studies of Pyrococcus furiosus superoxide reductase: implications for active-site structures and the catalytic mechanism. Clay, M.D., Jenney, F.E., Hagedoorn, P.L., George, G.N., Adams, M.W., Johnson, M.K. J. Am. Chem. Soc. (2002) [Pubmed]
  5. Geometries and electronic structures of cyanide adducts of the non-heme iron active site of superoxide reductases: vibrational and ENDOR studies. Clay, M.D., Yang, T.C., Jenney, F.E., Kung, I.Y., Cosper, C.A., Krishnan, R., Kurtz, D.M., Adams, M.W., Hoffman, B.M., Johnson, M.K. Biochemistry (2006) [Pubmed]
  6. Production of a thermostable archaeal superoxide reductase in plant cells. Im, Y.J., Ji, M., Lee, A.M., Boss, W.F., Grunden, A.M. FEBS Lett. (2005) [Pubmed]
  7. Mössbauer characterization of an unusual high-spin side-on peroxo-Fe3+ species in the active site of superoxide reductase from Desulfoarculus Baarsii. Density functional calculations on related models. Horner, O., Mouesca, J.M., Oddou, J.L., Jeandey, C., Nivière, V., Mattioli, T.A., Mathé, C., Fontecave, M., Maldivi, P., Bonville, P., Halfen, J.A., Latour, J.M. Biochemistry (2004) [Pubmed]
  8. The first crystal structure of class III superoxide reductase from Treponema pallidum. Santos-Silva, T., Trincão, J., Carvalho, A.L., Bonifácio, C., Auchère, F., Raleiras, P., Moura, I., Moura, J.J., Romão, M.J. J. Biol. Inorg. Chem. (2006) [Pubmed]
  9. In vitro reconstitution of an NADPH-dependent superoxide reduction pathway from Pyrococcus furiosus. Grunden, A.M., Jenney, F.E., Ma, K., Ji, M., Weinberg, M.V., Adams, M.W. Appl. Environ. Microbiol. (2005) [Pubmed]
 
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