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Volumn 51, Issue 5, 2012, Pages 974-985

The diheme cytochrome c peroxidase from Shewanella oneidensis requires reductive activation

Author keywords

[No Author keywords available]

Indexed keywords

ABSORBANCES; ACTIVATION RATES; DIHEME CYTOCHROME C; ELECTRON DONORS; ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY; IN-SITU; KINETIC MODELS; LAG PHASE; LOOP REGIONS; MICHAELIS-MENTEN; MICHAELIS-MENTEN KINETIC; PROGRESS CURVES; REDUCTIVE ACTIVATION; SEQUENCE ALIGNMENTS; SHEWANELLA ONEIDENSIS; STRUCTURAL BASIS; UV-VISIBLE;

EID: 84856734698     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201135s     Document Type: Article
Times cited : (36)

References (42)
  • 2
    • 0026740508 scopus 로고
    • Biologically relevant metal ion-dependent hydroxyl radical generation. An update
    • Halliwell, B. and Gutteridge, J. M. C. (1992) Biologically relevant metal ion-dependent hydroxyl radical generation. An update FEBS Lett. 307, 108-112
    • (1992) FEBS Lett. , vol.307 , pp. 108-112
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 3
    • 0031037665 scopus 로고    scopus 로고
    • FnrP and NNR of Paracoccus denitrificans are both members of the FNR family of transcriptional activators but have distinct roles in respiratory adaptation in response to oxygen limitation
    • Van Spanning, R. J., De Boer, A. P., Reijnders, W. N., Westerhoff, H. V., Stouthamer, A. H., and Van Der Oost, J. (1997) FnrP and NNR of Paracoccus denitrificans are both members of the FNR family of transcriptional activators but have distinct roles in respiratory adaptation in response to oxygen limitation Mol. Microbiol. 23, 893-907 (Pubitemid 27096726)
    • (1997) Molecular Microbiology , vol.23 , Issue.5 , pp. 893-907
    • Van Spanning, R.J.M.1    De Boer, A.P.N.2    Reijnders, W.N.M.3    Westerhoff, H.V.4    Stouthamer, A.H.5    Van Der Oost, J.6
  • 5
    • 0021723457 scopus 로고
    • Crystal structure of yeast cytochrome c peroxidase refined at 1.7-Å resolution
    • Finzel, B. C., Poulos, T. L., and Kraut, J. (1984) Crystal structure of yeast cytochrome c peroxidase refined at 1.7-Å resolution J. Biol. Chem. 259, 13027-13036 (Pubitemid 15223817)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.21 , pp. 13027-13036
    • Finzel, B.C.1    Poulos, T.L.2    Kraut, J.3
  • 7
    • 33645885635 scopus 로고    scopus 로고
    • Structure and mechanism in the bacterial dihaem cytochrome c peroxidases
    • Pettigrew, G. W., Echalier, A., and Pauleta, S. R. (2006) Structure and mechanism in the bacterial dihaem cytochrome c peroxidases J. Inorg. Biochem. 100, 551-567
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 551-567
    • Pettigrew, G.W.1    Echalier, A.2    Pauleta, S.R.3
  • 8
    • 0033574705 scopus 로고    scopus 로고
    • The structure of an electron transfer complex containing a cytochrome c and a peroxidase
    • Pettigrew, G. W., Prazeres, S., Costa, C., Palma, N., Krippahl, L., Moura, I., and Moura, J. J. (1999) The structure of an electron transfer complex containing a cytochrome c and a peroxidase J. Biol. Chem. 274, 11383-11389
    • (1999) J. Biol. Chem. , vol.274 , pp. 11383-11389
    • Pettigrew, G.W.1    Prazeres, S.2    Costa, C.3    Palma, N.4    Krippahl, L.5    Moura, I.6    Moura, J.J.7
  • 9
    • 10744222048 scopus 로고    scopus 로고
    • Electron Transfer Complexes of Cytochrome c Peroxidase from Paracoccus denitrificans Containing more than One Cytochrome
    • DOI 10.1021/bi034829c
    • Pettigrew, G. W., Pauleta, S. R., Goodhew, C. F., Cooper, A., Nutley, M., Jumel, K., Harding, S. E., Costa, C., Krippahl, L., Moura, I., and Moura, J. (2003) Electron transfer complexes of cytochrome c peroxidase from Paracoccus denitrificans containing more than one cytochrome Biochemistry 42, 11968-11981 (Pubitemid 37280647)
    • (2003) Biochemistry , vol.42 , Issue.41 , pp. 11968-11981
    • Pettigrew, G.W.1    Pauleta, S.R.2    Goodhew, C.F.3    Cooper, A.4    Nutley, M.5    Jumel, K.6    Harding, S.E.7    Costa, C.8    Krippahl, L.9    Moura, I.10    Moura, J.11
  • 10
    • 0018133520 scopus 로고
    • Pseudomonas cytochrome c peroxidase. Initial delay of the peroxidatic reaction. Electron transfer properties
    • Ronnberg, M. and Ellfolk, N. (1978) Pseudomonas cytochrome c peroxidase. Initial delay of the peroxidatic reaction. Electron transfer properties Biochim. Biophys. Acta 504, 60-66 (Pubitemid 9033868)
    • (1978) Biochimica et Biophysica Acta , vol.504 , Issue.1 , pp. 60-66
    • Ronnberg, M.1    Ellfolk, N.2
  • 11
    • 33644795665 scopus 로고    scopus 로고
    • Activation and catalysis of the di-heme cytochrome c peroxidase from Paracoccus pantotrophus
    • DOI 10.1016/j.str.2005.09.011, PII S0969212605003904
    • Echalier, A., Goodhew, C. F., Pettigrew, G. W., and Fulop, V. (2006) Activation and catalysis of the di-heme cytochrome c peroxidase from Paracoccus pantotrophus Structure 14, 107-117 (Pubitemid 43350078)
    • (2006) Structure , vol.14 , Issue.1 , pp. 107-117
    • Echalier, A.1    Goodhew, C.F.2    Pettigrew, G.W.3    Fulop, V.4
  • 12
    • 39649109897 scopus 로고    scopus 로고
    • Redox-linked structural changes associated with the formation of a catalytically competent form of the diheme cytochrome c peroxidase from Pseudomonas aeruginosa
    • DOI 10.1021/bi702064f
    • Echalier, A., Brittain, T., Wright, J., Boycheva, S., Mortuza, G. B., Fulop, V., and Watmough, N. J. (2008) Redox-linked structural changes associated with the formation of a catalytically competent form of the diheme cytochrome c peroxidase from Pseudomonas aeruginosa Biochemistry 47, 1947-1956 (Pubitemid 351287120)
    • (2008) Biochemistry , vol.47 , Issue.7 , pp. 1947-1956
    • Echalier, A.1    Brittain, T.2    Wright, J.3    Boycheva, S.4    Mortuza, G.B.5    Fulop, V.6    Watmough, N.J.7
  • 13
    • 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
    • DOI 10.1021/bi011481h
    • Shimizu, H., Schuller, D. J., Lanzilotta, W. N., Sundaramoorthy, M., Arciero, D. M., Hooper, A. B., and Poulos, T. L. (2001) Crystal structure of Nitrosomonas europaea cytochrome c peroxidase and the structural basis for ligand switching in bacterial di-heme peroxidases Biochemistry 40, 13483-13490 (Pubitemid 33130776)
    • (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
  • 14
    • 0028317005 scopus 로고
    • The kinetics of the oxidation of cytochrome c by Paracoccus cytochrome c peroxidase
    • Gilmour, R., Goodhew, C. F., Pettigrew, G. W., Prazeres, S., Moura, J. J. G., and Moura, I. (1994) The kinetics of the oxidation of cytochrome c by Paracoccus cytochrome c peroxidase Biochem. J. 300, 907-914 (Pubitemid 24180611)
    • (1994) Biochemical Journal , vol.300 , Issue.3 , pp. 907-914
    • Gilmour, R.1    Goodhew, C.F.2    Pettigrew, G.W.3    Prazeres, S.4    Moura, J.J.G.5    Moura, I.6
  • 16
    • 0035663745 scopus 로고    scopus 로고
    • Cloning, overproduction and characterization of cytochrome c peroxidase from the purple phototrophic bacterium Rhodobacter capsulatus
    • DOI 10.1046/j.0014-2956.2001.02610.x
    • De Smet, L., Pettigrew, G. W., and Van Beeumen, J. J. (2001) Cloning, overproduction and characterization of cytochrome c peroxidase from the purple phototrophic bacterium Rhodobacter capsulatus Eur. J. Biochem. 268, 6559-6568 (Pubitemid 34014763)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.24 , pp. 6559-6568
    • De Smet, L.1    Pettigrew, G.W.2    Van Beeumen, J.J.3
  • 18
    • 70349813787 scopus 로고    scopus 로고
    • CcpA from Geobacter sulfurreducens is a basic di-heme cytochrome c peroxidase
    • Hoffmann, M., Seidel, J., and Einsle, O. (2009) CcpA from Geobacter sulfurreducens is a basic di-heme cytochrome c peroxidase J. Mol. Biol. 393, 951-965
    • (2009) J. Mol. Biol. , vol.393 , pp. 951-965
    • Hoffmann, M.1    Seidel, J.2    Einsle, O.3
  • 19
    • 0028235802 scopus 로고
    • A di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically active in both the oxidized and half-reduced states
    • Arciero, D. and Hooper, A. B. (1994) A di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically active in both the oxidized and half-reduced states J. Biol. Chem. 269, 11878-11886 (Pubitemid 24196676)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.16 , pp. 11878-11886
    • Arciero, D.M.1    Hooper, A.B.2
  • 21
    • 52949132999 scopus 로고    scopus 로고
    • Addressing Shewanella oneidensis 'cytochromome': The first step towards high-throughput expression of cytochromes c
    • Londer, Y. Y., Giuliani, S. E., Peppler, T., and Collart, F. R. (2008) Addressing Shewanella oneidensis 'cytochromome': The first step towards high-throughput expression of cytochromes c Protein Expression Purif. 62, 128-137
    • (2008) Protein Expression Purif. , vol.62 , pp. 128-137
    • Londer, Y.Y.1    Giuliani, S.E.2    Peppler, T.3    Collart, F.R.4
  • 23
    • 23544450428 scopus 로고
    • The extinction coefficient of cytochrome c
    • Van Gelder, B. and Slater, E. C. (1962) The extinction coefficient of cytochrome c Biochim. Biophys. Acta 58, 593-595
    • (1962) Biochim. Biophys. Acta , vol.58 , pp. 593-595
    • Van Gelder, B.1    Slater, E.C.2
  • 24
    • 0015476272 scopus 로고
    • Pseudomonas cytochrome c peroxidase. IV. Some kinetic properties of the peroxidations reaction, and enzymatic determination of the extinction coefficients of Pseudomonas cytochrome c-551 and azurin
    • Soininen, R. and Ellfolk, N. (1972) Pseudomonas cytochrome c peroxidase. IV. Some kinetic properties of the peroxidations reaction, and enzymatic determination of the extinction coefficients of Pseudomonas cytochrome c-551 and azurin Acta Chem. Scand. 26, 861-872
    • (1972) Acta Chem. Scand. , vol.26 , pp. 861-872
    • Soininen, R.1    Ellfolk, N.2
  • 25
    • 0037199442 scopus 로고    scopus 로고
    • Differential effect of a His tag at the N- and C-termini: Functional studies with recombinant human serum transferrin
    • DOI 10.1021/bi025927l
    • Mason, A. B., He, Q. Y., Halbrooks, P. J., Everse, S. J., Gumerov, D. R., Kaltashov, I. A., Smith, V. C., Hewitt, J., and MacGillivray, R. T. A. (2002) Differential effect of a his tag at the N- and C-termini: Functional studies with recombinant human serum transferrin Biochemistry 41, 9448-9454 (Pubitemid 34810020)
    • (2002) Biochemistry , vol.41 , Issue.30 , pp. 9448-9454
    • Mason, A.B.1    He, Q.-Y.2    Halbrooks, P.J.3    Everse, S.J.4    Gumerov, D.R.5    Kaltashov, I.A.6    Smith, V.C.7    Hewitt, J.8    MacGillivray, R.T.A.9
  • 26
    • 33847714692 scopus 로고    scopus 로고
    • Cautionary tail: The presence of an N-terminal tag on dynein light-chain roadblock/LC7 affects its interaction with a functional partner
    • DOI 10.2174/092986607780090801
    • Song, J. and Markley, J. L. (2007) Cautionary tail: The presence of an N-terminal tag on dynein light-chain Roadblock/LC7 affects its interaction with a functional partner Protein Pept. Lett. 14, 265-268 (Pubitemid 46376858)
    • (2007) Protein and Peptide Letters , vol.14 , Issue.3 , pp. 265-268
    • Song, J.1    Markley, J.L.2
  • 27
    • 0025045910 scopus 로고
    • The cellular location and specificity of bacterial cytochrome c peroxidases
    • Goodhew, C. F., Wilson, I. B., Hunter, D. J., and Pettigrew, G. W. (1990) The cellular location and specificity of bacterial cytochrome c peroxidases Biochem. J. 271, 707-712 (Pubitemid 20384605)
    • (1990) Biochemical Journal , vol.271 , Issue.3 , pp. 707-712
    • Goodhew, C.F.1    Wilson, I.B.2    Hunter, D.J.B.3    Pettigrew, G.W.4
  • 29
    • 0027489230 scopus 로고
    • Spectroscopic characterization of cytochrome c peroxidase from Paracoccus denitrificans
    • Gilmour, R., Goodhew, C. F., Pettigrew, G. W., Prazeres, S., Moura, I., and Moura, J. J. (1993) Spectroscopic characterization of cytochrome c peroxidase from Paracoccus denitrificans Biochem. J. 294, 745-752 (Pubitemid 23286562)
    • (1993) Biochemical Journal , vol.294 , Issue.3 , pp. 745-752
    • Gilmour, R.1    Goodhew, C.F.2    Pettigrew, G.W.3    Prazeres, S.4    Moura, I.5    Moura, J.J.G.6
  • 30
    • 0022410920 scopus 로고
    • Redox-linked spin-state changes in the di-haem cytochrome c-551 peroxidase from Pseudomonas aeruginosa
    • Foote, N., Peterson, J., Gadsby, P., Greenwood, C., and Thomson, A. (1985) Redox-linked spin-state changes in the di-haem cytochrome c-551 peroxidase from Pseudomonas aeruginosa Biochem. J. 230, 227-237 (Pubitemid 16247289)
    • (1985) Biochemical Journal , vol.230 , Issue.1 , pp. 227-237
    • Foote, N.1    Peterson, J.2    Gadsby, P.M.A.3
  • 31
    • 0028972074 scopus 로고
    • Mossbauer characterization of Paracoccus denitrificans cytochrome c peroxidase. Further evidence for redox and calcium binding-induced heme-heme interaction
    • Prazeres, S., Moura, J. J., Moura, I., Gilmour, R., Goodhew, C. F., Pettigrew, G. W., Ravi, N., and Huynh, B. H. (1995) Mossbauer characterization of Paracoccus denitrificans cytochrome c peroxidase. Further evidence for redox and calcium binding-induced heme-heme interaction J. Biol. Chem. 270, 24264-24269
    • (1995) J. Biol. Chem. , vol.270 , pp. 24264-24269
    • Prazeres, S.1    Moura, J.J.2    Moura, I.3    Gilmour, R.4    Goodhew, C.F.5    Pettigrew, G.W.6    Ravi, N.7    Huynh, B.H.8
  • 32
    • 0019775732 scopus 로고
    • Electron paramagnetic resonance studies of Pseudomonas cytochrome c peroxidase
    • Aasa, R., Ellfolk, N., Ronnberg, M., and Vanngard, T. (1981) Electron paramagnetic resonance studies of Pseudomonas cytochrome c peroxidase Biochim. Biophys. Acta 670, 170-175 (Pubitemid 12193146)
    • (1981) Biochimica et Biophysica Acta , vol.670 , Issue.2 , pp. 170-175
    • Aasa, R.1    Ellfolk, N.2    Ronnberg, M.3    Vanngard, T.4
  • 33
    • 0021764425 scopus 로고
    • A study of the oxidized form of Pseudomonas aeruginosa cytochrome c-551 peroxidase with the use of magnetic circular dichroism
    • Foote, N., Peterson, J., Gadsby, P. M., Greenwood, C., and Thomson, A. J. (1984) A study of the oxidized form of Pseudomonas aeruginosa cytochrome c-551 peroxidase with the use of magnetic circular dichroism Biochem. J. 223, 369-378
    • (1984) Biochem. J. , vol.223 , pp. 369-378
    • Foote, N.1    Peterson, J.2    Gadsby, P.M.3    Greenwood, C.4    Thomson, A.J.5
  • 35
    • 0017593566 scopus 로고
    • The EPR of low spin heme complexes: Relation of the tau2g hole model to the directional properties of the g tensor, and a new method for calculating the ligand field parameters
    • Taylor, C. (1977) The EPR of low spin heme complexes: Relation of the tau2g hole model to the directional properties of the g tensor, and a new method for calculating the ligand field parameters Biochim. Biophys. Acta 491, 137-148
    • (1977) Biochim. Biophys. Acta , vol.491 , pp. 137-148
    • Taylor, C.1
  • 39
    • 0026559952 scopus 로고
    • A quantitative model for the mechanism of action of the cytochrome c peroxidase of Pseudomonas aeruginosa
    • Foote, N., Turner, R., Brittain, T., and Greenwood, C. (1992) A quantitative model for the mechanism of action of the cytochrome c peroxidase of Pseudomonas aeruginosa Biochem. J. 283, 839-843
    • (1992) Biochem. J. , vol.283 , pp. 839-843
    • Foote, N.1    Turner, R.2    Brittain, T.3    Greenwood, C.4
  • 40
    • 33645238281 scopus 로고    scopus 로고
    • Structural and mutagenesis studies on the cytochrome c peroxidase from Rhodobacter capsulatus provide new insights into structure-function relationships of bacterial di-heme peroxidases
    • DOI 10.1074/jbc.M509582200
    • De Smet, L., Savvides, S. N., Van Horen, E., Pettigrew, G., and Van Beeumen, J. J. (2006) Structural and mutagenesis studies on the cytochrome c peroxidase from Rhodobacter capsulatus provide new insights into structure-function relationships of bacterial di-heme peroxidases J. Biol. Chem. 281, 4371-4379 (Pubitemid 43847869)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.7 , pp. 4371-4379
    • De Smet, L.1    Savvides, S.N.2    Van Horen, E.3    Pettigrew, G.4    Van Beeumen, J.J.5
  • 41
    • 34347387298 scopus 로고    scopus 로고
    • Activation of the cytochrome c peroxidase of Pseudomonas aeruginosa. The role of a heme-linked protein loop: A mutagenesis studies
    • DOI 10.1016/j.jinorgbio.2007.04.012, PII S0162013407000840
    • Hsiao, H.-C., Boycheva, S., Watmough, N. J., and Brittain, T. (2007) Activation of the cytochrome c peroxidase of Pseudomonas aeruginosa. The role of a heme-linked protein loop: A mutagenesis study J. Biol. Inorg. Chem. 101, 1133-1139 (Pubitemid 47021204)
    • (2007) Journal of Inorganic Biochemistry , vol.101 , Issue.8 , pp. 1133-1139
    • Hsiao, H.-C.1    Boycheva, S.2    Watmough, N.J.3    Brittain, T.4
  • 42
    • 80052714737 scopus 로고    scopus 로고
    • Investigation of the Electron Transport Chain to and the Catalytic Activity of the Diheme Cytochrome c Peroxidase CcpA of Shewanella oneidensis
    • Schütz, B., Seidel, J., Sturm, G., Einsle, O., and Gescher, J. (2011) Investigation of the Electron Transport Chain to and the Catalytic Activity of the Diheme Cytochrome c Peroxidase CcpA of Shewanella oneidensis. Appl. Environ. Microbiol. 77, 6172-6180
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 6172-6180
    • Schütz, B.1    Seidel, J.2    Sturm, G.3    Einsle, O.4    Gescher, J.5


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