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UQCRFS1  -  ubiquinol-cytochrome c reductase, Rieske...

Bos taurus

 
 
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Disease relevance of UQCRFS1

 

High impact information on UQCRFS1

  • The destruction of the Rieske iron-sulfur cluster ([2Fe-2S]) in the bc(1) complex by hematoporphyrin-promoted photoinactivation resulted in the complex becoming proton-permeable [4].
  • The crystal structure of the bovine Rieske iron-sulfur protein indicates a sulfur atom (S-1) of the iron-sulfur cluster and the sulfur atom (Sgamma) of a cysteine residue that coordinates one of the iron atoms form hydrogen bonds with the hydroxyl groups of Ser-163 and Tyr-165, respectively [5].
  • The amino acid sequence of subunit 9 of the bovine heart cytochrome bc1 complex is identical to the 78-amino acid presequence that is removed post-translationally from the Rieske iron-sulfur protein as it is imported and targeted to the mitochondrial cytochrome bc1 complex [6].
  • The spin relaxation of the Rieske iron-sulfur cluster was enhanced by the paramagnetic cytochrome c1 and b566 hemes but not by cytochrome b562 [7].
  • Negatively charged residues and hydrogen bonds tune the ligand histidine pKa values of Rieske iron-sulfur proteins [8].
 

Biological context of UQCRFS1

 

Anatomical context of UQCRFS1

 

Associations of UQCRFS1 with chemical compounds

 

Other interactions of UQCRFS1

 

Analytical, diagnostic and therapeutic context of UQCRFS1

References

  1. Inhibition of electron transfer by 3-alkyl-2-hydroxy-1,4-naphthoquinones in the ubiquinol-cytochrome c oxidoreductases of Rhodopseudomonas sphaeroides and mammalian mitochondria. Interaction with a ubiquinone-binding site and the Rieske iron-sulfur cluster. Matsuura, K., Bowyer, J.R., Ohnishi, T., Dutton, P.L. J. Biol. Chem. (1983) [Pubmed]
  2. Conserved nonliganding residues of the Rhodobacter capsulatus Rieske iron-sulfur protein of the bc1 complex are essential for protein structure, properties of the [2Fe-2S] cluster, and communication with the quinone pool. Liebl, U., Sled, V., Brasseur, G., Ohnishi, T., Daldal, F. Biochemistry (1997) [Pubmed]
  3. Mutational analysis of residues forming hydrogen bonds in the Rieske [2Fe-2S] cluster of the cytochrome bc1 complex in Paracoccus denitrificans. Schröter, T., Hatzfeld, O.M., Gemeinhardt, S., Korn, M., Friedrich, T., Ludwig, B., Link, T.A. Eur. J. Biochem. (1998) [Pubmed]
  4. The iron-sulfur cluster of the Rieske iron-sulfur protein functions as a proton-exiting gate in the cytochrome bc(1) complex. Gurung, B., Yu, L., Xia, D., Yu, C.A. J. Biol. Chem. (2005) [Pubmed]
  5. Alteration of the midpoint potential and catalytic activity of the rieske iron-sulfur protein by changes of amino acids forming hydrogen bonds to the iron-sulfur cluster. Denke, E., Merbitz-Zahradnik, T., Hatzfeld, O.M., Snyder, C.H., Link, T.A., Trumpower, B.L. J. Biol. Chem. (1998) [Pubmed]
  6. The mitochondrial targeting presequence of the Rieske iron-sulfur protein is processed in a single step after insertion into the cytochrome bc1 complex in mammals and retained as a subunit in the complex. Brandt, U., Yu, L., Yu, C.A., Trumpower, B.L. J. Biol. Chem. (1993) [Pubmed]
  7. Spatial organization of redox active centers in the bovine heart ubiquinol-cytochrome c oxidoreductase. Ohnishi, T., Schägger, H., Meinhardt, S.W., LoBrutto, R., Link, T.A., von Jagow, G. J. Biol. Chem. (1989) [Pubmed]
  8. Negatively charged residues and hydrogen bonds tune the ligand histidine pKa values of Rieske iron-sulfur proteins. Klingen, A.R., Ullmann, G.M. Biochemistry (2004) [Pubmed]
  9. Cloning and sequencing of a cDNA encoding the Rieske iron-sulfur protein of bovine heart mitochondrial ubiquinol-cytochrome c reductase. Usui, S., Yu, L., Yu, C.A. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  10. Orientation of the g-tensor axes of the Rieske subunit in the cytochrome bc1 complex. Bowman, M.K., Berry, E.A., Roberts, A.G., Kramer, D.M. Biochemistry (2004) [Pubmed]
  11. Effects of 2-hydroxy-3-undecyl-1,4-naphthoquinone on respiration of electron transport particles and mitochondria: topographical location of the Rieske iron-sulfur protein and the quinone binding site. Harmon, H.J., Struble, V.G. Biochemistry (1983) [Pubmed]
  12. Mitochondrial ubiquinol-cytochrome c reductase complex: crystallization and protein: ubiquinone interaction. Yu, C.A., Yu, L. J. Bioenerg. Biomembr. (1993) [Pubmed]
  13. The oxidation of ubiquinol by the isolated Rieske iron-sulfur protein in solution. DegliEsposti, M., Ballester, F., Timoneda, J., Crimi, M., Lenaz, G. Arch. Biochem. Biophys. (1990) [Pubmed]
  14. Use of a photoactivated ruthenium dimer complex to measure electron transfer between the Rieske iron-sulfur protein and cytochrome c(1) in the cytochrome bc(1) complex. Sadoski, R.C., Engstrom, G., Tian, H., Zhang, L., Yu, C.A., Yu, L., Durham, B., Millett, F. Biochemistry (2000) [Pubmed]
  15. Effect of ethoxyformic anhydride on the Rieske iron-sulfur protein of bovine heart ubiquinol: cytochrome c oxidoreductase. Ohnishi, T., Meinhardt, S.W., von Jagow, G., Yagi, T., Hatefi, Y. FEBS Lett. (1994) [Pubmed]
  16. Structure and reaction mechanisms of multifunctional mitochondrial cytochrome bc1 complex. Yu, C.A., Zhang, L., Deng, K.P., Tian, H., Xia, D., Kim, H., Deisenhofer, J., Yu, L. Biofactors (1999) [Pubmed]
  17. Characterization and crystallization of the lumen side domain of the chloroplast Rieske iron-sulfur protein. Zhang, H., Carrell, C.J., Huang, D., Sled, V., Ohnishi, T., Smith, J.L., Cramer, W.A. J. Biol. Chem. (1996) [Pubmed]
 
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