The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
MeSH Review

Paracoccus

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of Paracoccus

 

High impact information on Paracoccus

  • Using the enzyme cytochrome c oxidase aa3 from the bacterium Paracoccus denitrificans, we have studied haem dynamics during the photo-initiated ultrafast transfer of carbon monoxide from haem a3 to CuB by femtosecond spectroscopy [6].
  • The complex is composed of three electron transfer proteins from Paracoccus denitrificans, the quinoprotein methylamine dehydrogenase, the blue copper protein amicyanin, and the cytochrome c551i [7].
  • We have deleted the COIII gene from Paracoccus denitrificans [8].
  • Cytochrome cd1 nitrite reductase (cd1) from Paracoccus pantotrophus is a respiratory enzyme capable of using nitrite, hydroxylamine and oxygen as electron accepting substrates [9].
  • The crystal structures of cytochrome c oxidase from both bovine and Paracoccus denitrificans reveal two putative proton input channels that connect the heme-copper center, where dioxygen is reduced, to the internal aqueous phase [10].
 

Chemical compound and disease context of Paracoccus

  • 13N- and 15N-labeling experiments were carried out with Paracoccus denitrificans, grown anaerobically on nitrate, to determine whether hyponitrite might be an obligatory intermediate in denitrification and a precursor of nitrous oxide [11].
  • A cytochrome ba3 functions as a quinol oxidase in Paracoccus denitrificans. Purification, cloning, and sequence comparison [12].
  • Tryptophan 121 of subunit II is the electron entry site to cytochrome-c oxidase in Paracoccus denitrificans. Involvement of a hydrophobic patch in the docking reaction [13].
  • The crystal structures of glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans, which catalyzes the formation of S-hydroxymethylglutathione from formaldehyde and glutathione, and its complex with glutathione (Gfa-GTT) have been determined [14].
  • However, unlike the mitochondrial complexes, which contain eight to 11 polypeptides and are thought to contain distinct quinone binding proteins, the Paracoccus cytochrome bc1 complex contains only three polypeptide subunits, cytochromes b, c1, and iron-sulfur protein [15].
 

Biological context of Paracoccus

 

Anatomical context of Paracoccus

 

Gene context of Paracoccus

  • COX10 codes for a protein homologous to the ORF1 product of Paracoccus denitrificans and is required for the synthesis of yeast cytochrome oxidase [25].
  • We have used a bacterial counterpart of Complex I, NDH-1 from Paracoccus denitrificans, for studying the effect of mutations in the ND1 subunit on the enzymatic activity [26].
  • The transcription factor NNR from Paracoccus denitrificans was expressed in a strain of Escherichia coli carrying a plasmid-borne fusion of the melR promoter to lacZ, with a consensus FNR-binding site 41.5 bp upstream of the transcription start site [27].
  • Identification of the contiguous Paracoccus denitrificans ccmF and ccmH genes: disruption of ccmF, encoding a putative transporter, results in formation of an unstable apocytochrome c and deficiency in siderophore production [28].
  • In previous reports from our laboratory, the three structural genes (NQO1, NQO2, and NQO3) of the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans were characterized [Xu, X., Matsuno-Yagi, A., & Yagi, T. (1991) Biochemistry 30, 6422-6428; (1991) Biochemistry 30, 8678-8684; (1992) Arch. Biochem. Biophys. 296, 40-48] [29].
 

Analytical, diagnostic and therapeutic context of Paracoccus

  • Here, we demonstrate that the crystallization of the cytochrome c oxidase from Paracoccus denitrificans can be mediated by co-crystallization with an antibody Fv fragment [30].
  • Resonance Raman and Fourier transform infrared spectroscopies have been used to study the aa(3)-type cytochrome c oxidase and the Y280H mutant from Paracoccus denitrificans [31].
  • Cloning and sequence analysis of cycH gene from Paracoccus denitrificans: the cycH gene product is required for assembly of all c-type cytochromes, including cytochrome c1 [32].
  • The structural changes in the heme macrocycle and substituents caused by binding of Ca(2+) to the diheme cytochrome c peroxidase from Paracoccus pantotrophus were clarified by resonance Raman spectroscopy of the inactive fully oxidized form of the enzyme [33].
  • Redox dependent changes at the heme propionates in cytochrome c oxidase from Paracoccus denitrificans: direct evidence from FTIR difference spectroscopy in combination with heme propionate 13C labeling [34].

References

  1. Ion selectivity reversal and induction of voltage-gating by site-directed mutations in the Paracoccus denitrificans porin. Saxena, K., Drosou, V., Maier, E., Benz, R., Ludwig, B. Biochemistry (1999) [Pubmed]
  2. 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]
  3. Structural aspects of the dye-linked alcohol dehydrogenase of Rhodopseudomonas acidophila. Bamforth, C.W., Quayle, J.R. Biochem. J. (1979) [Pubmed]
  4. The biochemical characterization of a novel non-haem-iron hydroxylamine oxidase from Paracoccus denitrificans GB17. Moir, J.W., Wehrfritz, J.M., Spiro, S., Richardson, D.J. Biochem. J. (1996) [Pubmed]
  5. 19F-nuclear magnetic resonance: measurements of [O2] and pH in biological systems. Taylor, J., Deutsch, C. Biophys. J. (1988) [Pubmed]
  6. Coherent reaction dynamics in a bacterial cytochrome c oxidase. Liebl, U., Lipowski, G., Négrerie, M., Lambry, J.C., Martin, J.L., Vos, M.H. Nature (1999) [Pubmed]
  7. Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i. Chen, L., Durley, R.C., Mathews, F.S., Davidson, V.L. Science (1994) [Pubmed]
  8. Deletion of the gene for subunit III leads to defective assembly of bacterial cytochrome oxidase. Haltia, T., Finel, M., Harms, N., Nakari, T., Raitio, M., Wikström, M., Saraste, M. EMBO J. (1989) [Pubmed]
  9. A switch in heme axial ligation prepares Paracoccus pantotrophus cytochrome cd1 for catalysis. Allen, J.W., Watmough, N.J., Ferguson, S.J. Nat. Struct. Biol. (2000) [Pubmed]
  10. The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer. Konstantinov, A.A., Siletsky, S., Mitchell, D., Kaulen, A., Gennis, R.B. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  11. 13N,15N isotope and kinetic evidence against hyponitrite as an intermediate in dentrification. Hollocher, T.C., Garber, E., Cooper, A.J., Reiman, R.E. J. Biol. Chem. (1980) [Pubmed]
  12. A cytochrome ba3 functions as a quinol oxidase in Paracoccus denitrificans. Purification, cloning, and sequence comparison. Richter, O.M., Tao, J.S., Turba, A., Ludwig, B. J. Biol. Chem. (1994) [Pubmed]
  13. Tryptophan 121 of subunit II is the electron entry site to cytochrome-c oxidase in Paracoccus denitrificans. Involvement of a hydrophobic patch in the docking reaction. Witt, H., Malatesta, F., Nicoletti, F., Brunori, M., Ludwig, B. J. Biol. Chem. (1998) [Pubmed]
  14. A dynamic zinc redox switch. Neculai, A.M., Neculai, D., Griesinger, C., Vorholt, J.A., Becker, S. J. Biol. Chem. (2005) [Pubmed]
  15. Identification of a stable ubisemiquinone and characterization of the effects of ubiquinone oxidation-reduction status on the Rieske iron-sulfur protein in the three-subunit ubiquinol-cytochrome c oxidoreductase complex of Paracoccus denitrificans. Meinhardt, S.W., Yang, X.H., Trumpower, B.L., Ohnishi, T. J. Biol. Chem. (1987) [Pubmed]
  16. EPR characterization of the iron-sulfur clusters in the NADH: ubiquinone oxidoreductase segment of the respiratory chain in Paracoccus denitrificans. Meinhardt, S.W., Kula, T., Yagi, T., Lillich, T., Ohnishi, T. J. Biol. Chem. (1987) [Pubmed]
  17. Structure and kinetic properties of Paracoccus pantotrophus cytochrome cd1 nitrite reductase with the d1 heme active site ligand tyrosine 25 replaced by serine. Gordon, E.H., Sjögren, T., Löfqvist, M., Richter, C.D., Allen, J.W., Higham, C.W., Hajdu, J., Fülöp, V., Ferguson, S.J. J. Biol. Chem. (2003) [Pubmed]
  18. Nitric oxide reacts with the single-electron reduced active site of cytochrome c oxidase. Giuffrè, A., Barone, M.C., Brunori, M., D'Itri, E., Ludwig, B., Malatesta, F., Müller, H.W., Sarti, P. J. Biol. Chem. (2002) [Pubmed]
  19. The genes of the Paracoccus denitrificans bc1 complex. Nucleotide sequence and homologies between bacterial and mitochondrial subunits. Kurowski, B., Ludwig, B. J. Biol. Chem. (1987) [Pubmed]
  20. Transcription regulation of the nir gene cluster encoding nitrite reductase of Paracoccus denitrificans involves NNR and NirI, a novel type of membrane protein. Saunders, N.F., Houben, E.N., Koefoed, S., de Weert, S., Reijnders, W.N., Westerhoff, H.V., De Boer, A.P., Van Spanning, R.J. Mol. Microbiol. (1999) [Pubmed]
  21. Nitric oxide reductase. Purification from Paracoccus denitrificans with use of a single column and some characteristics. Dermastia, M., Turk, T., Hollocher, T.C. J. Biol. Chem. (1991) [Pubmed]
  22. A bacterial c-type cytochrome can be translocated to the periplasm as an apo form; the biosynthesis of cytochrome cd1 (nitrite reductase) from Paracoccus denitrificans. Page, M.D., Ferguson, S.J. Mol. Microbiol. (1989) [Pubmed]
  23. The location of dissimilatory nitrite reductase and the control of dissimilatory nitrate reductase by oxygen in Paracoccus denitrificans. Alefounder, P.R., Ferguson, S.J. Biochem. J. (1980) [Pubmed]
  24. Unidirectional effect of lauryl sulfate on the reversible NADH:ubiquinone oxidoreductase (Complex I). Grivennikova, V.G., Ushakova, A.V., Cecchini, G., Vinogradov, A.D. FEBS Lett. (2003) [Pubmed]
  25. COX10 codes for a protein homologous to the ORF1 product of Paracoccus denitrificans and is required for the synthesis of yeast cytochrome oxidase. Nobrega, M.P., Nobrega, F.G., Tzagoloff, A. J. Biol. Chem. (1990) [Pubmed]
  26. Analysis of the pathogenic human mitochondrial mutation ND1/3460, and mutations of strictly conserved residues in its vicinity, using the bacterium Paracoccus denitrificans. Zickermann, V., Barquera, B., Wikström, M., Finel, M. Biochemistry (1998) [Pubmed]
  27. Heterologous NNR-mediated nitric oxide signaling in Escherichia coli. Hutchings, M.I., Shearer, N., Wastell, S., van Spanning, R.J., Spiro, S. J. Bacteriol. (2000) [Pubmed]
  28. Identification of the contiguous Paracoccus denitrificans ccmF and ccmH genes: disruption of ccmF, encoding a putative transporter, results in formation of an unstable apocytochrome c and deficiency in siderophore production. Pearce, D.A., Page, M.D., Norris, H.A., Tomlinson, E.J., Ferguson, S.J. Microbiology (Reading, Engl.) (1998) [Pubmed]
  29. Gene cluster of the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans: characterization of four structural gene products. Xu, X., Matsuno-Yagi, A., Yagi, T. Biochemistry (1992) [Pubmed]
  30. Fv fragment-mediated crystallization of the membrane protein bacterial cytochrome c oxidase. Ostermeier, C., Iwata, S., Ludwig, B., Michel, H. Nat. Struct. Biol. (1995) [Pubmed]
  31. The role of the cross-link His-Tyr in the functional properties of the binuclear center in cytochrome c oxidase. Pinakoulaki, E., Pfitzner, U., Ludwig, B., Varotsis, C. J. Biol. Chem. (2002) [Pubmed]
  32. Cloning and sequence analysis of cycH gene from Paracoccus denitrificans: the cycH gene product is required for assembly of all c-type cytochromes, including cytochrome c1. Page, M.D., Ferguson, S.J. Mol. Microbiol. (1995) [Pubmed]
  33. Calcium-dependent conformation of a heme and fingerprint peptide of the diheme cytochrome c peroxidase from Paracoccus pantotrophus. Pauleta, S.R., Lu, Y., Goodhew, C.F., Moura, I., Pettigrew, G.W., Shelnutt, J.A. Biochemistry (2001) [Pubmed]
  34. Redox dependent changes at the heme propionates in cytochrome c oxidase from Paracoccus denitrificans: direct evidence from FTIR difference spectroscopy in combination with heme propionate 13C labeling. Behr, J., Hellwig, P., Mäntele, W., Michel, H. Biochemistry (1998) [Pubmed]
 
WikiGenes - Universities