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Gene Review

snr1  -  cytochrome C Snr1

Pseudomonas aeruginosa PAO1

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Disease relevance of snr1


High impact information on snr1

  • Treatment of mast cells with P. aeruginosa induced release of cytochrome c from mitochondria and loss of mitochondrial membrane potentials [5].
  • Cytochrome c reductase assays and electron paramagnetic resonance data show that electron transfer between the two proteins is pH-dependent and that the [3Fe-4S]+ cluster of FdI is specifically reduced by NADPH via FPR, suggesting that the [3Fe-4S] cluster is near FAD in the complex [6].
  • Subunit II was a triheme cytochrome c and had no enzyme activity, but it enabled the subunit I/III complex to reproduce the Q1 and ferricyanide reductase activities [3].
  • The complementing fragments have been isolated from the derived complexes and four apofragments and one heme fragment have been identified in the amino acid sequence of cytochrome c. They are (39-104), (40-104), (54-104), (56-104), and (1-53)H [7].
  • It has been hypothesised that the dihemic c4-Ps may have evolved via monohemic cytochrome c gene duplication followed by evolutionary divergence and the adjunction of a connecting linker [8].

Chemical compound and disease context of snr1


Biological context of snr1

  • Within the frame of the characterization of the structure and function of cytochromes c, an 81-amino acid cytochrome c was identified in the genome of Shewanella putrefaciens [14].
  • In our previous report, it was proposed that P. aeruginosa secreting ExoS, upon infection, shuts down host cell survival signal pathways by inhibiting ERK1/2 and p38 activation, and it activates proapoptotic pathways through activation of JNK1/2, leading ultimately to cytochrome c release and activation of caspases [15].
  • Electrostatic effects on the kinetics of photoinduced electron-transfer reactions of the triplet state of zinc cytochrome c with wild-type and mutant forms of Pseudomonas aeruginosa azurin [16].

Anatomical context of snr1


Associations of snr1 with chemical compounds

  • The analysis strongly suggests that ionization of a haem propionate of mitochondrial cytochrome c triggers the alkaline conformation change [19].
  • Cytochrome c appears to be able to feed electrons into the chain at the level of one of the [4Fe-4S] centres of NiR [20].
  • The preparations vary in the amount of contaminating nitrate reductase, the amount of cytochrome c present and the concentration of oxidized [3Fe-4S] cluster [21].
  • High pH also displaces the methionine ligand in a manner similar to the well-known alkaline transition of mitochondrial cytochrome c. However, the reaction occurs at higher pH values and over a narrower pH range for the c-551 family, and the transition pH range is different for the different proteins studied [22].
  • NADH-cytochrome c reductase was inhibited by totarol while cytochrome c oxidase was not [23].

Other interactions of snr1

  • The visible-absorption spectra of the enzyme closely resemble those of cytochrome c peroxidase from Pseudomonas aeruginosa but the donor specificity is different, with the Pa. denitrificans enzyme preferring the basic mitochondrial cytochromes c to the acidic cytochromes c-551 and reacting well with the Pa. denitrificans cytochrome c-550 [17].

Analytical, diagnostic and therapeutic context of snr1


  1. Ligand binding to cytochrome c peroxidase from Pseudomonas aeruginosa. Greenwood, C., Gibson, Q.H. J. Biol. Chem. (1989) [Pubmed]
  2. A di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically active in both the oxidized and half-reduced states. Arciero, D.M., Hooper, A.B. J. Biol. Chem. (1994) [Pubmed]
  3. Function of multiple heme c moieties in intramolecular electron transport and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-cytochrome c complex of Gluconobacter suboxydans. Matsushita, K., Yakushi, T., Toyama, H., Shinagawa, E., Adachi, O. J. Biol. Chem. (1996) [Pubmed]
  4. Structural characterization of Paracoccus denitrificans cytochrome c peroxidase and assignment of the low and high potential heme sites. Hu, W., Van Driessche, G., Devreese, B., Goodhew, C.F., McGinnity, D.F., Saunders, N., Fulop, V., Pettigrew, G.W., Van Beeumen, J.J. Biochemistry (1997) [Pubmed]
  5. Pseudomonas aeruginosa-Induced Human Mast Cell Apoptosis Is Associated with Up-Regulation of Endogenous Bcl-xS and Down-Regulation of Bcl-xL. Jenkins, C.E., Swiatoniowski, A., Power, M.R., Lin, T.J. J. Immunol. (2006) [Pubmed]
  6. Complex formation between Azotobacter vinelandii ferredoxin I and its physiological electron donor NADPH-ferredoxin reductase. Jung, Y.S., Roberts, V.A., Stout, C.D., Burgess, B.K. J. Biol. Chem. (1999) [Pubmed]
  7. Formation of a biologically active, ordered complex from two overlapping fragments of cytochrome c. Hantgan, R.R., Taniuchi, H. J. Biol. Chem. (1977) [Pubmed]
  8. MAD structure of Pseudomonas nautica dimeric cytochrome c552 mimicks the c4 Dihemic cytochrome domain association. Brown, K., Nurizzo, D., Besson, S., Shepard, W., Moura, J., Moura, I., Tegoni, M., Cambillau, C. J. Mol. Biol. (1999) [Pubmed]
  9. The reaction of Pseudomonas aeruginosa cytochrome c oxidase with carbon monoxide. Parr, S.R., Wilson, M.T., Greenwood, C. Biochem. J. (1975) [Pubmed]
  10. Quaternary structure of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa and its reoxidation with a novel cytochrome c from this organism. Schrover, J.M., Frank, J., van Wielink, J.E., Duine, J.A. Biochem. J. (1993) [Pubmed]
  11. Partial purification and characterization of thiosulfate oxidase from Pseudomonas aeruginosa. Schook, L.B., Berk, R.S. J. Bacteriol. (1979) [Pubmed]
  12. A rapid-scan spectrometric and stopped-flow study of compound I and compound II of Pseudomonas cytochrome c peroxidase. Rönnberg, M., Lambeir, A.M., Ellfolk, N., Dunford, H.B. Arch. Biochem. Biophys. (1985) [Pubmed]
  13. Effect of water-miscible organic solvents on the catalytic activity of cytochrome c. Vazquez-Duhalt, R., Semple, K.M., Westlake, D.W., Fedorak, P.M. Enzyme Microb. Technol. (1993) [Pubmed]
  14. Solution structure of a monoheme ferrocytochrome c from Shewanella putrefaciens and structural analysis of sequence-similar proteins: functional implications. Bartalesi, I., Bertini, I., Hajieva, P., Rosato, A., Vasos, P.R. Biochemistry (2002) [Pubmed]
  15. Expression of Pseudomonas aeruginosa Toxin ExoS Effectively Induces Apoptosis in Host Cells. Jia, J., Wang, Y., Zhou, L., Jin, S. Infect. Immun. (2006) [Pubmed]
  16. Electrostatic effects on the kinetics of photoinduced electron-transfer reactions of the triplet state of zinc cytochrome c with wild-type and mutant forms of Pseudomonas aeruginosa azurin. Sokerina, E.V., Ullmann, G.M., van Pouderoyen, G., Canters, G.W., Kostić, N.M. J. Biol. Inorg. Chem. (1999) [Pubmed]
  17. The cellular location and specificity of bacterial cytochrome c peroxidases. Goodhew, C.F., Wilson, I.B., Hunter, D.J., Pettigrew, G.W. Biochem. J. (1990) [Pubmed]
  18. Investigation of Helicobacter pylori ascorbic acid oxidating activity. Odum, L., Andersen, L.P. FEMS Immunol. Med. Microbiol. (1995) [Pubmed]
  19. Fourier-transform infra-red studies of the alkaline isomerization of mitochondrial cytochrome c and the ionization of carboxylic acids. Tonge, P., Moore, G.R., Wharton, C.W. Biochem. J. (1989) [Pubmed]
  20. Electron-paramagnetic-resonance and magnetic-circular-dichroism studies on the formate dehydrogenase-nitrate reductase particle from Pseudomonas aeruginosa. Godfrey, C., Gadsby, P.M., Thomson, A.J., Greenwood, C., Coddington, A. Biochem. J. (1987) [Pubmed]
  21. Purification and properties of formate dehydrogenase from Pseudomonas aeruginosa. Characterization of haem and iron-sulphur centres by magnetic-circular-dichroism and electron-paramagnetic-resonance spectroscopy. Godfrey, C., Coddington, A., Greenwood, C., Thomson, A.J., Gadsby, P.M. Biochem. J. (1987) [Pubmed]
  22. Heme crevice disorder after sixth ligand displacement in the cytochrome c-551 family. Chen, Y., Liang, Q., Arciero, D.M., Hooper, A.B., Timkovich, R. Arch. Biochem. Biophys. (2007) [Pubmed]
  23. Mode of antibacterial action of totarol, a diterpene from Podocarpus nagi. Haraguchi, H., Oike, S., Muroi, H., Kubo, I. Planta Med. (1996) [Pubmed]
  24. The reaction between reduced azurin and oxidized cytochrome c peroxidase from Pseudomonas aeruginosa. Ronnberg, M., Araiso, T., Ellfolk, N., Dunford, H.B. J. Biol. Chem. (1981) [Pubmed]
  25. Crystallization and preliminary X-ray analysis of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa. Fülöp, V., Little, R., Thompson, A., Greenwood, C., Hajdu, J. J. Mol. Biol. (1993) [Pubmed]
  26. Electron transfer from Phanerochaete chrysosporium cellobiose oxidase to equine cytochrome c and Pseudomonas aeruginosa cytochrome c-551. Rogers, M.S., Jones, G.D., Antonini, G., Wilson, M.T., Brunori, M. Biochem. J. (1994) [Pubmed]
  27. Characterization of temporal protein production in Pseudomonas aeruginosa biofilms. Southey-Pillig, C.J., Davies, D.G., Sauer, K. J. Bacteriol. (2005) [Pubmed]
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