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Volumn 581, Issue 5, 2007, Pages 911-916

Cytochromes P460 and c′-beta; A new family of high-spin cytochromes c

Author keywords

Bacterial enzyme evolution; Cytochrome c ; Cytochrome P460; Denitrification; N oxide detoxification

Indexed keywords

CYTOCHROME C; CYTOCHROME C' BETA; CYTOCHROME P460; UNCLASSIFIED DRUG;

EID: 33847129611     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.01.068     Document Type: Article
Times cited : (49)

References (41)
  • 1
    • 0015514077 scopus 로고
    • Preliminary characterization of a variant CO-binding heme protein from Nitrosomonas
    • Erickson R.H., and Hooper A.B. Preliminary characterization of a variant CO-binding heme protein from Nitrosomonas. Biochim. Biophys. Acta 275 (1972) 231-244
    • (1972) Biochim. Biophys. Acta , vol.275 , pp. 231-244
    • Erickson, R.H.1    Hooper, A.B.2
  • 2
    • 0028131263 scopus 로고
    • Oxidation of hydroxylamine by cytochrome P-460 of the obligate methylotroph Methylococcus capsulatus Bath
    • Zahn J., Duncan C., and DiSpirito A. Oxidation of hydroxylamine by cytochrome P-460 of the obligate methylotroph Methylococcus capsulatus Bath. J. Bacteriol. 176 19 (1994) 5879-5887
    • (1994) J. Bacteriol. , vol.176 , Issue.19 , pp. 5879-5887
    • Zahn, J.1    Duncan, C.2    DiSpirito, A.3
  • 3
    • 0021734180 scopus 로고
    • Further characterization of cytochrome P-460 in Nitrosomonas europaea
    • Miller D.A., Wood P.M., and Nicholas D.J.D. Further characterization of cytochrome P-460 in Nitrosomonas europaea. J. Gen. Microbiol. 130 (1984) 3049-3054
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 3049-3054
    • Miller, D.A.1    Wood, P.M.2    Nicholas, D.J.D.3
  • 4
    • 0025613888 scopus 로고
    • Cytochrome P-460 of Nitrosomonas europaea: further purification and further characterization
    • (Tokyo)
    • Numata M., Saito T., Yamazaki T., Fukumori Y., and Yamanaka T. Cytochrome P-460 of Nitrosomonas europaea: further purification and further characterization. J. Biochem. 108 6 (1990) 1016-1021 (Tokyo)
    • (1990) J. Biochem. , vol.108 , Issue.6 , pp. 1016-1021
    • Numata, M.1    Saito, T.2    Yamazaki, T.3    Fukumori, Y.4    Yamanaka, T.5
  • 5
    • 0028046264 scopus 로고
    • The primary structure of cytochrome P460 of Nitrosomonas europaea: Presence of a c-heme binding motif
    • Bergmann D.J., and Hooper A.B. The primary structure of cytochrome P460 of Nitrosomonas europaea: Presence of a c-heme binding motif. FEBS Lett. 353 3 (1994) 324-326
    • (1994) FEBS Lett. , vol.353 , Issue.3 , pp. 324-326
    • Bergmann, D.J.1    Hooper, A.B.2
  • 6
    • 0030833664 scopus 로고    scopus 로고
    • Evidence for a crosslink between c-heme and a lysine residue in cytochrome P460 of Nitrosomonas europaea
    • Arciero D.M., and Hooper A.B. Evidence for a crosslink between c-heme and a lysine residue in cytochrome P460 of Nitrosomonas europaea. FEBS Lett. 410 2-3 (1997) 457-460
    • (1997) FEBS Lett. , vol.410 , Issue.2-3 , pp. 457-460
    • Arciero, D.M.1    Hooper, A.B.2
  • 7
    • 0027445613 scopus 로고
    • Evidence for the structure of the active site heme P460 in hydroxylamine oxidoreductase of Nitrosomonas
    • Arciero D.M., Hooper A.B., Cai M., and Timkovich R. Evidence for the structure of the active site heme P460 in hydroxylamine oxidoreductase of Nitrosomonas. Biochemistry 32 36 (1993) 9370-9378
    • (1993) Biochemistry , vol.32 , Issue.36 , pp. 9370-9378
    • Arciero, D.M.1    Hooper, A.B.2    Cai, M.3    Timkovich, R.4
  • 8
    • 0030611275 scopus 로고    scopus 로고
    • The 2.8 Å structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea
    • Igarashi N., Moriyama H., Fujiwara T., Fukumori Y., and Tanaka N. The 2.8 Å structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea. Nat. Struct. Biol. 4 (1997) 276-284
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 276-284
    • Igarashi, N.1    Moriyama, H.2    Fujiwara, T.3    Fukumori, Y.4    Tanaka, N.5
  • 10
    • 0021287328 scopus 로고
    • Mossbauer, EPR, and optical studies of the P-460 center of hydroxylamine oxidoreductase from Nitrosomonas. A ferrous heme with an unusually large quadrupole splitting
    • Andersson K., Kent T., Lipscomb J., Hooper A., and Munck E. Mossbauer, EPR, and optical studies of the P-460 center of hydroxylamine oxidoreductase from Nitrosomonas. A ferrous heme with an unusually large quadrupole splitting. J. Biol. Chem. 259 11 (1984) 6833-6840
    • (1984) J. Biol. Chem. , vol.259 , Issue.11 , pp. 6833-6840
    • Andersson, K.1    Kent, T.2    Lipscomb, J.3    Hooper, A.4    Munck, E.5
  • 12
    • 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., Anderson B.F., Faber H.R., and Baker E.N. Three-dimensional structure of cytochrome c′ from two Alcaligenes species and the implications for four-helix bundle structures. Acta Crystallogr. D Biol. Crystallogr. 52 (1996) 356-368
    • (1996) Acta Crystallogr. D Biol. Crystallogr. , vol.52 , pp. 356-368
    • Dobbs, A.J.1    Anderson, B.F.2    Faber, H.R.3    Baker, E.N.4
  • 13
    • 0029892085 scopus 로고    scopus 로고
    • Concerted movement of side chains in the haem vicinity observed on ligand binding in cytochrome c′ from Rhodobacter capsulatus
    • Tahirov T.H., Misaki S., Meyer T.E., Cusanovich M.A., Higuchi Y., and Yasuoka N. Concerted movement of side chains in the haem vicinity observed on ligand binding in cytochrome c′ from Rhodobacter capsulatus. Nat. Struct. Biol. 3 (1996) 459-464
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 459-464
    • Tahirov, T.H.1    Misaki, S.2    Meyer, T.E.3    Cusanovich, M.A.4    Higuchi, Y.5    Yasuoka, N.6
  • 15
    • 0032431903 scopus 로고    scopus 로고
    • Cytochrome P460 genes from the methanotroph Methylococcus capsulatus Bath
    • Bergmann D.J., Zahn J.A., Hooper A.B., and DiSpirito A.A. Cytochrome P460 genes from the methanotroph Methylococcus capsulatus Bath. J. Bacteriol. 180 24 (1998) 6440-6445
    • (1998) J. Bacteriol. , vol.180 , Issue.24 , pp. 6440-6445
    • Bergmann, D.J.1    Zahn, J.A.2    Hooper, A.B.3    DiSpirito, A.A.4
  • 16
    • 0033972007 scopus 로고    scopus 로고
    • Primary structure of cytochrome c′ of Methylococcus capsulatus Bath: Evidence of a phylogenetic link between P460 and c′-type cytochromes
    • Bergmann D.J., Zahn J.A., and DiSpirito A.A. Primary structure of cytochrome c′ of Methylococcus capsulatus Bath: Evidence of a phylogenetic link between P460 and c′-type cytochromes. Arch. Microbiol. 173 (2000) 29-34
    • (2000) Arch. Microbiol. , vol.173 , pp. 29-34
    • Bergmann, D.J.1    Zahn, J.A.2    DiSpirito, A.A.3
  • 17
    • 0038030009 scopus 로고    scopus 로고
    • Cytochrome P460 of Nitrosomonas europaea. Formation of the heme-lysine cross-link in a heterologous host and mutagenic conversion to a non-cross-linked cytochrome c′
    • Bergmann D.J., and Hooper A.B. Cytochrome P460 of Nitrosomonas europaea. Formation of the heme-lysine cross-link in a heterologous host and mutagenic conversion to a non-cross-linked cytochrome c′. Eur. J. Biochem. 270 (2003) 1935-1941
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1935-1941
    • Bergmann, D.J.1    Hooper, A.B.2
  • 18
    • 33847149936 scopus 로고    scopus 로고
    • Elmore, B., Bergmann, D., Klotz, M. and Hooper, A.B. (2006) Cytochromes-P460 and c′, a New Class of High-Spin c-Cytochromes Differing from the "Classic" Alpha-Helical cytochromes c'. In: Proceedings of 106th General Meeting of the American Society for Microbiology, May 21-25, 2006. Orlando, Florida. ISBN 1-55581-389-5.
  • 20
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucl. Acids Res. 25 (1997) 4876-4882
    • (1997) Nucl. Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 21
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai K., and Horton P. PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem. Sci. 24 1 (1999) 34-35
    • (1999) Trends Biochem. Sci. , vol.24 , Issue.1 , pp. 34-35
    • Nakai, K.1    Horton, P.2
  • 23
    • 0035861456 scopus 로고    scopus 로고
    • Bayesian inference of phylogeny and its impact on evolutionary biology
    • Huelsenbeck J.P., Ronquist F., Nielsen R., and Bollback J.P. Bayesian inference of phylogeny and its impact on evolutionary biology. Science 294 (2001) 2310-2314
    • (2001) Science , vol.294 , pp. 2310-2314
    • Huelsenbeck, J.P.1    Ronquist, F.2    Nielsen, R.3    Bollback, J.P.4
  • 24
    • 0041386108 scopus 로고    scopus 로고
    • MRBAYES 3: Bayesian phylogenetic inference under mixed models
    • Ronquist F., and Huelsenbeck J.P. MRBAYES 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19 (2003) 1572-1574
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 25
    • 0035031966 scopus 로고    scopus 로고
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach
    • Whelan S., and Goldman N. A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach. Mol. Biol. Evol. 18 (2001) 691-699
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 691-699
    • Whelan, S.1    Goldman, N.2
  • 26
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin L.J., Bryson K., and Jones D.T. The PSIPRED protein structure prediction server. Bioinformatics 16 (2000) 404-405
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 27
    • 0025008168 scopus 로고
    • Sequence logos: a new way to display consensus sequences
    • Schneider T.D., and Stephens R.M. Sequence logos: a new way to display consensus sequences. Nucl. Acids Res. 18 (1990) 6097-6100
    • (1990) Nucl. Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2
  • 28
    • 33645771950 scopus 로고    scopus 로고
    • Expression, purification, crystallization and preliminary X-ray diffraction of a novel Nitrosomonas europaea cytochrome, cytochrome P460
    • Elmore B.O., Pearson A.R., Wilmot C.M., and Hooper A.B. Expression, purification, crystallization and preliminary X-ray diffraction of a novel Nitrosomonas europaea cytochrome, cytochrome P460. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. 62 (2006) 395-398
    • (2006) Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. , vol.62 , pp. 395-398
    • Elmore, B.O.1    Pearson, A.R.2    Wilmot, C.M.3    Hooper, A.B.4
  • 29
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield N., and Fasman G.D. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8 (1969) 4108-4116
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 30
    • 0015870378 scopus 로고
    • Circular dichroism and optical rotatory dispersion of proteins and polypeptides
    • Adler A.J., Greenfield N.J., and Fasman G.D. Circular dichroism and optical rotatory dispersion of proteins and polypeptides. Methods Enzymol. 27 (1973) 675-735
    • (1973) Methods Enzymol. , vol.27 , pp. 675-735
    • Adler, A.J.1    Greenfield, N.J.2    Fasman, G.D.3
  • 32
    • 0031734953 scopus 로고    scopus 로고
    • Heme packing motifs revealed by the crystal structure of the tetra-heme cytochrome c554 from Nitrosomonas europaea
    • Iverson T.M., Arciero D.M., Hsu B.T., Logan M.S.P., Hooper A.B., and Rees D.C. Heme packing motifs revealed by the crystal structure of the tetra-heme cytochrome c554 from Nitrosomonas europaea. Nat. Struct. Biol. 5 11 (1998) 1005-1012
    • (1998) Nat. Struct. Biol. , vol.5 , Issue.11 , pp. 1005-1012
    • Iverson, T.M.1    Arciero, D.M.2    Hsu, B.T.3    Logan, M.S.P.4    Hooper, A.B.5    Rees, D.C.6
  • 33
    • 0035856525 scopus 로고    scopus 로고
    • Crystal structure of Nitrosomonas europaea cytochrome c peroxidase and the structural basis for ligand switching in bacterial di-heme peroxidases
    • Shimizu H., Schuller D.J., Lanzilotta W.N., Sundaramoorthy M., Arciero D.M., Hooper A.B., and Poulos T.L. Crystal structure of Nitrosomonas europaea cytochrome c peroxidase and the structural basis for ligand switching in bacterial di-heme peroxidases. Biochemistry 40 45 (2001) 13483-13490
    • (2001) Biochemistry , vol.40 , Issue.45 , pp. 13483-13490
    • Shimizu, H.1    Schuller, D.J.2    Lanzilotta, W.N.3    Sundaramoorthy, M.4    Arciero, D.M.5    Hooper, A.B.6    Poulos, T.L.7
  • 34
    • 0028773015 scopus 로고
    • Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation
    • Martinez S.E., Huang D., Szczepaniak A., Cramer W.A., and Smith J.L. Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation. Structure 2 (1994) 95-105
    • (1994) Structure , vol.2 , pp. 95-105
    • Martinez, S.E.1    Huang, D.2    Szczepaniak, A.3    Cramer, W.A.4    Smith, J.L.5
  • 35
    • 0242494128 scopus 로고    scopus 로고
    • Structure of the cytochrome b6f complex of oxygenic photosynthesis: Tuning the cavity
    • Kurisu G., Zhang H., Smith J.L., and Cramer W.A. Structure of the cytochrome b6f complex of oxygenic photosynthesis: Tuning the cavity. Science 302 (2003) 1009-1014
    • (2003) Science , vol.302 , pp. 1009-1014
    • Kurisu, G.1    Zhang, H.2    Smith, J.L.3    Cramer, W.A.4
  • 38
    • 0035030166 scopus 로고    scopus 로고
    • Enzymatic removal of nitric oxide catalyzed by cytochrome c′ in Rhodobacter capsulatus
    • Cross R., Lloyd D., Poole R.K., and Moir J.W. Enzymatic removal of nitric oxide catalyzed by cytochrome c′ in Rhodobacter capsulatus. J. Bacteriol. 183 (2001) 3050-3054
    • (2001) J. Bacteriol. , vol.183 , pp. 3050-3054
    • Cross, R.1    Lloyd, D.2    Poole, R.K.3    Moir, J.W.4
  • 39
    • 19744380767 scopus 로고    scopus 로고
    • Nitric oxide detoxification systems enhance survival of Neisseria meningitidis in human macrophages and in nasopharyngeal mucosa
    • Stevanin T.M., Moir J.W., and Read R.C. Nitric oxide detoxification systems enhance survival of Neisseria meningitidis in human macrophages and in nasopharyngeal mucosa. Infect. Immunol. 73 (2005) 3322-3329
    • (2005) Infect. Immunol. , vol.73 , pp. 3322-3329
    • Stevanin, T.M.1    Moir, J.W.2    Read, R.C.3
  • 41
    • 25144469781 scopus 로고    scopus 로고
    • Structure and sequence conservation of hao cluster genes of autotrophic ammonia-oxidizing bacteria: evidence for their evolutionary history
    • Bergmann D.J., Hooper A.B., and Klotz M.G. Structure and sequence conservation of hao cluster genes of autotrophic ammonia-oxidizing bacteria: evidence for their evolutionary history. Appl. Environ. Microbiol. 71 (2005) 5371-5382
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 5371-5382
    • Bergmann, D.J.1    Hooper, A.B.2    Klotz, M.G.3


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