메뉴 건너뛰기




Volumn 182, Issue 5, 2000, Pages 1442-1447

Cytochrome c' from Rhodobacter capsulatus confers increased resistance to nitric oxide

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CYTOCHROME C'; NITRIC OXIDE; NITROSO DERIVATIVE; OXYGEN; THIOL DERIVATIVE; UNCLASSIFIED DRUG;

EID: 0033965782     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.5.1442-1447.2000     Document Type: Article
Times cited : (59)

References (31)
  • 2
    • 0022455510 scopus 로고
    • Relative rates of nitric oxide and nitrous oxide production by nitrifiers, denitrifiers, and nitrate respirers
    • Anderson, I. C., and J. S. Levine. 1986. Relative rates of nitric oxide and nitrous oxide production by nitrifiers, denitrifiers, and nitrate respirers. Appl. Environ. Microbiol. 51:938-945.
    • (1986) Appl. Environ. Microbiol. , vol.51 , pp. 938-945
    • Anderson, I.C.1    Levine, J.S.2
  • 3
    • 0024654435 scopus 로고
    • Nucleotide sequence, organization, and nature of the protein products of the carotenoid biosynthesis gene cluster of Rhodobacter capsulatus
    • Armstrong, G. A., M. Alberti, F. Leach, and J. E. Hearst. 1989. Nucleotide sequence, organization, and nature of the protein products of the carotenoid biosynthesis gene cluster of Rhodobacter capsulatus. Mol. Gen. Genet. 216: 254-268.
    • (1989) Mol. Gen. Genet. , vol.216 , pp. 254-268
    • Armstrong, G.A.1    Alberti, M.2    Leach, F.3    Hearst, J.E.4
  • 6
    • 0029980044 scopus 로고    scopus 로고
    • Inhibition of nitric oxide synthase attenuates blood-brain barrier disruption during experimental meningitis
    • Boje, K. M. K. 1996. Inhibition of nitric oxide synthase attenuates blood-brain barrier disruption during experimental meningitis. Brain Res. 720:75-83.
    • (1996) Brain Res. , vol.720 , pp. 75-83
    • Boje, K.M.K.1
  • 7
    • 0028134892 scopus 로고
    • Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase
    • Brown, G. C., and C. E. Cooper. 1994. Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase. FEBS Lett. 356:295-298.
    • (1994) FEBS Lett. , vol.356 , pp. 295-298
    • Brown, G.C.1    Cooper, C.E.2
  • 9
    • 0030046275 scopus 로고    scopus 로고
    • Three-dimensional structure of cytochrome c' from two Alcaligenes species and the implications for four-helix bundle structures
    • Dobbs, A. J., B. F. Anderson, H. R. Faber, and E. N. Baker. 1996. Three-dimensional structure of cytochrome c' from two Alcaligenes species and the implications for four-helix bundle structures. Acta Crystallogr. D52:356-368.
    • (1996) Acta Crystallogr. , vol.D52 , pp. 356-368
    • Dobbs, A.J.1    Anderson, B.F.2    Faber, H.R.3    Baker, E.N.4
  • 10
    • 0029095237 scopus 로고
    • Molecular-cloning and sequencing of cytochrome c' from the phototrophic purple sulfur bacterium Chromatium vinosum
    • Even, M. T., R. J. Kassner, M. Dolata, T. E. Meyer, and M. A. Cusanovich. 1995. Molecular-cloning and sequencing of cytochrome c' from the phototrophic purple sulfur bacterium Chromatium vinosum. Biochim. Biophys. Acta 1231:220-222.
    • (1995) . Biochim. Biophys. Acta , vol.1231 , pp. 220-222
    • Even, M.T.1    Kassner, R.J.2    Dolata, M.3    Meyer, T.E.4    Cusanovich, M.A.5
  • 11
    • 0022419653 scopus 로고
    • Structure of ferricytochrome c' from Rhodospirillum molischianum at 1.67 Å resolution
    • Finzel, B. C., P. C. Weber, K. D. Hardman, and F. R. Salemme. 1985. Structure of ferricytochrome c' from Rhodospirillum molischianum at 1.67 Å resolution. J. Mol. Biol. 186:627-643.
    • (1985) J. Mol. Biol. , vol.186 , pp. 627-643
    • Finzel, B.C.1    Weber, P.C.2    Hardman, K.D.3    Salemme, F.R.4
  • 13
    • 0029961489 scopus 로고    scopus 로고
    • Cloning of the lipooligosaccharide alpha-2,3-sialyltransferase from the bacterial pathogens Neisseria meningitidis and Neisseria gonorrhoeae
    • Gilbert, M., D. C. Watson, A. M. Cunningham, M. P. Jennings, N. M. Young, and W. W. Wakarchuk. 1996. Cloning of the lipooligosaccharide alpha-2,3-sialyltransferase from the bacterial pathogens Neisseria meningitidis and Neisseria gonorrhoeae. J. Biol. Chem. 271:28271-28276.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28271-28276
    • Gilbert, M.1    Watson, D.C.2    Cunningham, A.M.3    Jennings, M.P.4    Young, N.M.5    Wakarchuk, W.W.6
  • 16
    • 0023715368 scopus 로고
    • Improved broad-host-range plasmids for DNA cloning in Gram-negative bacteria
    • Keen, N. T., S. Tamaki, D. Kobayashi, and D. Trollinger. 1988. Improved broad-host-range plasmids for DNA cloning in Gram-negative bacteria. Gene 70:191-197.
    • (1988) Gene , vol.70 , pp. 191-197
    • Keen, N.T.1    Tamaki, S.2    Kobayashi, D.3    Trollinger, D.4
  • 17
    • 0017129914 scopus 로고
    • The spin 3/2 state and quantum spin mixtures in haem proteins
    • Maltempo, M. M., and T. H. Moss. 1976. The spin 3/2 state and quantum spin mixtures in haem proteins. Q. Rev. Biophys. 9:181-215.
    • (1976) Q. Rev. Biophys. , vol.9 , pp. 181-215
    • Maltempo, M.M.1    Moss, T.H.2
  • 18
    • 0031844664 scopus 로고    scopus 로고
    • A novel mechanism for upregulation of the Escherichia coli K-12 hmp (flavohaemoglobin) gene by the 'NO releaser,' S-nitrosoglutathione: Nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region
    • Membrillo-Hernandez, J., M. D. Coopamah, A. Channa, M. N. Hughes, and R. K. Poole. 1998. A novel mechanism for upregulation of the Escherichia coli K-12 hmp (flavohaemoglobin) gene by the 'NO releaser,' S-nitrosoglutathione: nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region. Mol. Microbiol. 29:1101-1112.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1101-1112
    • Membrillo-Hernandez, J.1    Coopamah, M.D.2    Channa, A.3    Hughes, M.N.4    Poole, R.K.5
  • 20
    • 0032997373 scopus 로고    scopus 로고
    • Cytochrome c' from paracoccus denitrificans: Spectroscopic studies consistent with a role for the protein in nitric oxide metabolism
    • Moir, J. W. B. 1999. Cytochrome c' from Paracoccus denitrificans: spectroscopic studies consistent with a role for the protein in nitric oxide metabolism. Biochim. Biophys. Acta 1430:65-72.
    • (1999) Biochim. Biophys. Acta , vol.1430 , pp. 65-72
    • Moir, J.W.B.1
  • 21
    • 0019469231 scopus 로고
    • Nucleotide sequence of the kanamycin resistance transposon Tn903
    • Oka, A., H. Sugisaki, and M. Takanami. 1981. Nucleotide sequence of the kanamycin resistance transposon Tn903. J. Mol. Biol. 147:217-226.
    • (1981) J. Mol. Biol. , vol.147 , pp. 217-226
    • Oka, A.1    Sugisaki, H.2    Takanami, M.3
  • 22
    • 0027380310 scopus 로고
    • Atomic-structure of a cytochrome c' with an unusual ligand-controlled dimer dissociation at 1.8 Å resolution
    • Ren, Z., T. Meyer, and D. E. McRee. 1993. Atomic-structure of a cytochrome c' with an unusual ligand-controlled dimer dissociation at 1.8 Å resolution. J. Mol. Biol. 234:433-445.
    • (1993) J. Mol. Biol. , vol.234 , pp. 433-445
    • Ren, Z.1    Meyer, T.2    McRee, D.E.3
  • 23
    • 0029667602 scopus 로고    scopus 로고
    • Flux between soil and atmosphere, vertical concentration profiles in soil, and turnover of nitric oxide. 2. Experiments with naturally layered soil cores
    • Rudolph, J., and R. Conrad. 1996. Flux between soil and atmosphere, vertical concentration profiles in soil, and turnover of nitric oxide. 2. Experiments with naturally layered soil cores. J. Atmos. Chem. 23:275-300.
    • (1996) J. Atmos. Chem. , vol.23 , pp. 275-300
    • Rudolph, J.1    Conrad, R.2
  • 24
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in Gram-negative bacteria
    • Simon, R., U. Priefer, and A. Puhler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram-negative bacteria. Bio/Technology 1:784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 25
    • 0029940242 scopus 로고    scopus 로고
    • High-resolution crystal structures of two polymorphs of cytochrome c' from the purple phototrophic bacterium Rhodobacter capsulatus
    • Tahirov, T. H., S. Misaki, T. E. Meyer, M. A. Cusanovich, Y. Higuchi, and N. Yasuoka. 1996. High-resolution crystal structures of two polymorphs of cytochrome c' from the purple phototrophic bacterium Rhodobacter capsulatus. J. Mol. Biol. 259:467-479.
    • (1996) J. Mol. Biol. , vol.259 , pp. 467-479
    • Tahirov, T.H.1    Misaki, S.2    Meyer, T.E.3    Cusanovich, M.A.4    Higuchi, Y.5    Yasuoka, N.6
  • 27
    • 0042345376 scopus 로고
    • Hematin compounds in photosynthetic bacteria
    • Vernon, L. P., and M. D. Kamen, 1954. Hematin compounds in photosynthetic bacteria. J. Biol. Chem. 211:643-662.
    • (1954) J. Biol. Chem. , vol.211 , pp. 643-662
    • Vernon, L.P.1    Kamen, M.D.2
  • 28
    • 0016720598 scopus 로고
    • Characterisation of Rhodopseudomonas capsulata
    • Weaver, P. F., J. D. Wall, and H. Gest. 1975. Characterisation of Rhodopseudomonas capsulata. Arch. Microbiol. 105:207-216.
    • (1975) Arch. Microbiol. , vol.105 , pp. 207-216
    • Weaver, P.F.1    Wall, J.D.2    Gest, H.3
  • 29
    • 0026598140 scopus 로고
    • 3-Dimensional structure of ferricytochrome c' from Rhodospirillum rubrum at 2.8 Å resolution
    • Yasui, M., S. Harada, Y. Kai, N. Kasai, M. Kusunoki, and Y. Matsuura. 1992. 3-Dimensional structure of ferricytochrome c' from Rhodospirillum rubrum at 2.8 Å resolution. J. Biochem. 111:317-324.
    • (1992) J. Biochem. , vol.111 , pp. 317-324
    • Yasui, M.1    Harada, S.2    Kai, Y.3    Kasai, N.4    Kusunoki, M.5    Matsuura, Y.6
  • 31
    • 0027360110 scopus 로고
    • 5 coordinated nitrosylhemoprotein in the whole cells of denitrifying bacterium, Achromobacter xylosoxidans NCIB 11015
    • Yoshimura, T., S. Shidara, T. Ozaki, and H. Kamada. 1993. 5 coordinated nitrosylhemoprotein in the whole cells of denitrifying bacterium, Achromobacter xylosoxidans NCIB 11015. Arch. Microbiol. 160:498-500.
    • (1993) Arch. Microbiol. , vol.160 , pp. 498-500
    • Yoshimura, T.1    Shidara, S.2    Ozaki, T.3    Kamada, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.