메뉴 건너뛰기




Volumn 64, Issue 4, 2007, Pages 1049-1060

A dedicated haem lyase is required for the maturation of a novel bacterial cytochrome c with unconventional covalent haem binding

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; CYTOCHROME C; LYASE;

EID: 34248342168     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2007.05712.x     Document Type: Article
Times cited : (48)

References (38)
  • 1
    • 0037072786 scopus 로고    scopus 로고
    • The Escherichia coli cytochrome c maturation (Ccm) system does not detectably attach heme to single cysteine variants of an apocytochrome c
    • Allen, J.W.A., Tomlinson, E.J., Hong, L. Ferguson, S.J. (2002) The Escherichia coli cytochrome c maturation (Ccm) system does not detectably attach heme to single cysteine variants of an apocytochrome c. J Biol Chem 277 : 33559 33563.
    • (2002) J Biol Chem , vol.277 , pp. 33559-33563
    • Allen, J.W.A.1    Tomlinson, E.J.2    Hong, L.3    Ferguson, S.J.4
  • 3
    • 9144261717 scopus 로고    scopus 로고
    • Maturation of the unusual single-cysteine (XXXCH) mitochondrial c-type cytochromes found in trypanosomatids must occur through a novel biogenesis pathway
    • Allen, J.W.A., Ginger, M.L. Ferguson, S.J. (2004) Maturation of the unusual single-cysteine (XXXCH) mitochondrial c-type cytochromes found in trypanosomatids must occur through a novel biogenesis pathway. Biochem J 383 : 537 542.
    • (2004) Biochem J , vol.383 , pp. 537-542
    • Allen, J.W.A.1    Ginger, M.L.2    Ferguson, S.J.3
  • 5
    • 22544463357 scopus 로고    scopus 로고
    • The histidine of the c-type cytochrome CXXCH haem-binding motif is essential for haem attachment by the Escherichia coli cytochrome c maturation (Ccm) apparatus
    • Allen, J.W.A., Leach, N. Ferguson, S.J. (2005b) The histidine of the c-type cytochrome CXXCH haem-binding motif is essential for haem attachment by the Escherichia coli cytochrome c maturation (Ccm) apparatus. Biochem J 389 : 587 592.
    • (2005) Biochem J , vol.389 , pp. 587-592
    • Allen, J.W.A.1    Leach, N.2    Ferguson, S.J.3
  • 7
    • 26444521691 scopus 로고    scopus 로고
    • Global transcriptome analysis of Shewanella oneidensis MR-1 exposed to different terminal electron acceptors
    • Beliaev, A.S., Klingeman, D.M., Klappenbach, J.A., Wu, L., Romine, M.F., Tiedje, J.M., et al. (2005) Global transcriptome analysis of Shewanella oneidensis MR-1 exposed to different terminal electron acceptors. J Bacteriol 187 : 7138 7145.
    • (2005) J Bacteriol , vol.187 , pp. 7138-7145
    • Beliaev, A.S.1    Klingeman, D.M.2    Klappenbach, J.A.3    Wu, L.4    Romine, M.F.5    Tiedje, J.M.6
  • 8
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • Berry, E.A. Trumpower, B.L. (1987) Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra. Anal Biochem 161 : 1 15.
    • (1987) Anal Biochem , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 9
    • 0033199635 scopus 로고    scopus 로고
    • Characterization of a flavocytochrome that is induced during the anaerobic respiration of Fe3+ by Shewanella frigidimarina NCIMB400
    • Dobbin, P.S., Butt, J.N., Powell, A.K., Reid, G.A. Richardson, D.J. (1999) Characterization of a flavocytochrome that is induced during the anaerobic respiration of Fe3+ by Shewanella frigidimarina NCIMB400. Biochem J 342 : 439 448.
    • (1999) Biochem J , vol.342 , pp. 439-448
    • Dobbin, P.S.1    Butt, J.N.2    Powell, A.K.3    Reid, G.A.4    Richardson, D.J.5
  • 10
    • 0037462683 scopus 로고    scopus 로고
    • Functional analysis of a divergent system II protein, Ccs1, involved in c-type cytochrome biogenesis
    • Dreyfuss, B.W., Hamel, P.P., Nakamoto, S.S. Merchant, S. (2003) Functional analysis of a divergent system II protein, Ccs1, involved in c-type cytochrome biogenesis. J Biol Chem 278 : 2604 2613.
    • (2003) J Biol Chem , vol.278 , pp. 2604-2613
    • Dreyfuss, B.W.1    Hamel, P.P.2    Nakamoto, S.S.3    Merchant, S.4
  • 11
    • 0031895861 scopus 로고    scopus 로고
    • Involvement of products of the nrfEFG genes in the covalent attachment of haem c to a novel cysteine-lysine motif in the cytochrome c552 nitrite reductase from Escherichia coli
    • Eaves, D.J., Grove, J., Staudenmann, W., James, P., Poole, R.K., White, S.A., et al. (1998) Involvement of products of the nrfEFG genes in the covalent attachment of haem c to a novel cysteine-lysine motif in the cytochrome c552 nitrite reductase from Escherichia coli. Mol Microbiol 28 : 205 216.
    • (1998) Mol Microbiol , vol.28 , pp. 205-216
    • Eaves, D.J.1    Grove, J.2    Staudenmann, W.3    James, P.4    Poole, R.K.5    White, S.A.6
  • 13
    • 33645809956 scopus 로고    scopus 로고
    • Recombinant cytochromes c biogenesis systems I and II and analysis of haem delivery pathways in Escherichia coli
    • Feissner, R.E., Richard-Fogal, C.L., Frawley, E.R., Loughman, J.A., Earley, K.W. Kranz, R.G. (2006) Recombinant cytochromes c biogenesis systems I and II and analysis of haem delivery pathways in Escherichia coli. Mol Microbiol 60 : 563 577.
    • (2006) Mol Microbiol , vol.60 , pp. 563-577
    • Feissner, R.E.1    Richard-Fogal, C.L.2    Frawley, E.R.3    Loughman, J.A.4    Earley, K.W.5    Kranz, R.G.6
  • 15
    • 46149130370 scopus 로고
    • Haem staining in gels, a useful tool in the study of bacterial c-type cytochromes
    • Goodhew, C.F., Brown, K.R. Pettigrew, G.W. (1986) Haem staining in gels, a useful tool in the study of bacterial c-type cytochromes. Biochim Biophys Acta 852 : 288 294.
    • (1986) Biochim Biophys Acta , vol.852 , pp. 288-294
    • Goodhew, C.F.1    Brown, K.R.2    Pettigrew, G.W.3
  • 16
    • 0037462720 scopus 로고    scopus 로고
    • Essential histidine and tryptophan residues in CcsA, a system II polytopic cytochrome c biogenesis protein
    • Hamel, P.P., Dreyfuss, B.W., Xie, Z., Gabilly, S.T. Merchant, S. (2003) Essential histidine and tryptophan residues in CcsA, a system II polytopic cytochrome c biogenesis protein. J Biol Chem 278 : 2593 2603.
    • (2003) J Biol Chem , vol.278 , pp. 2593-2603
    • Hamel, P.P.1    Dreyfuss, B.W.2    Xie, Z.3    Gabilly, S.T.4    Merchant, S.5
  • 17
    • 32544437414 scopus 로고    scopus 로고
    • Multiple haem lyase genes indicate substrate specificity in cytochrome c biogenesis
    • Hartshorne, S., Richardson, D.J. Simon, J. (2006) Multiple haem lyase genes indicate substrate specificity in cytochrome c biogenesis. Biochem Soc Trans 34 : 146 149.
    • (2006) Biochem Soc Trans , vol.34 , pp. 146-149
    • Hartshorne, S.1    Richardson, D.J.2    Simon, J.3
  • 18
    • 0031875674 scopus 로고    scopus 로고
    • Molecular mechanisms of cytochrome c biogenesis: Three distinct systems
    • Kranz, R., Lill, R., Goldman, B., Bonnard, G. Merchant, S. (1998) Molecular mechanisms of cytochrome c biogenesis: three distinct systems. Mol Microbiol 29 : 383 396.
    • (1998) Mol Microbiol , vol.29 , pp. 383-396
    • Kranz, R.1    Lill, R.2    Goldman, B.3    Bonnard, G.4    Merchant, S.5
  • 19
    • 0037122939 scopus 로고    scopus 로고
    • Fumarate respiration of Wolinella succinogenes: Enzymology, energetics and coupling mechanism
    • Kröger, A., Biel, S., Simon, J., Gross, R., Unden, G. Lancaster, C.R.D. (2002) Fumarate respiration of Wolinella succinogenes: enzymology, energetics and coupling mechanism. Biochim Biophys Acta 1553 : 23 38.
    • (2002) Biochim Biophys Acta , vol.1553 , pp. 23-38
    • Kröger, A.1    Biel, S.2    Simon, J.3    Gross, R.4    Unden, G.5    Lancaster, C.R.D.6
  • 20
    • 0027411256 scopus 로고
    • Regulation of anaerobic respiratory pathways in Wolinella succinogenes by the presence of electron acceptors
    • Lorenzen, J.P., Kröger, A. Unden, G. (1993) Regulation of anaerobic respiratory pathways in Wolinella succinogenes by the presence of electron acceptors. Arch Microbiol 159 : 477 483.
    • (1993) Arch Microbiol , vol.159 , pp. 477-483
    • Lorenzen, J.P.1    Kröger, A.2    Unden, G.3
  • 21
    • 33645568742 scopus 로고    scopus 로고
    • Heterologous production in Wolinella succinogenes and characterization of the quinol: Fumarate reductase enzymes from Helicobacter pylori and Campylobacter jejuni
    • Mileni, M., MacMillan, F., Tziatzios, C., Zwicker, K., Haas, A.H., Mäntele, W., et al. (2006) Heterologous production in Wolinella succinogenes and characterization of the quinol: fumarate reductase enzymes from Helicobacter pylori and Campylobacter jejuni. Biochem J 395 : 191 201.
    • (2006) Biochem J , vol.395 , pp. 191-201
    • Mileni, M.1    MacMillan, F.2    Tziatzios, C.3    Zwicker, K.4    Haas, A.H.5    Mäntele, W.6
  • 23
    • 27744493432 scopus 로고    scopus 로고
    • Multi-heme cytochromes - New structures, new chemistry
    • Mowat, C.G. Chapman, S.K. (2005) Multi-heme cytochromes - new structures, new chemistry. Dalton Trans 21 : 3381 3389.
    • (2005) Dalton Trans , vol.21 , pp. 3381-3389
    • Mowat, C.G.1    Chapman, S.K.2
  • 24
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D.N., Pappin, D.J., Creasy, D.M. Cottrell, J.S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20 : 3551 3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 25
    • 0036273999 scopus 로고    scopus 로고
    • The nrfI gene is essential for the attachment of the active site haem group of Wolinella succinogenes cytochrome c nitrite reductase
    • Pisa, R., Stein, T., Eichler, R., Gross, R. Simon, J. (2002) The nrfI gene is essential for the attachment of the active site haem group of Wolinella succinogenes cytochrome c nitrite reductase. Mol Microbiol 43 : 763 770.
    • (2002) Mol Microbiol , vol.43 , pp. 763-770
    • Pisa, R.1    Stein, T.2    Eichler, R.3    Gross, R.4    Simon, J.5
  • 27
    • 0036024581 scopus 로고    scopus 로고
    • Enzymology and bioenergetics of respiratory nitrite ammonification
    • Simon, J. (2002) Enzymology and bioenergetics of respiratory nitrite ammonification. FEMS Microbiol Rev 26 : 285 309.
    • (2002) FEMS Microbiol Rev , vol.26 , pp. 285-309
    • Simon, J.1
  • 28
    • 0032518289 scopus 로고    scopus 로고
    • Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon
    • Simon, J., Gross, R., Ringel, M., Schmidt, E. Kröger, A. (1998) Deletion and site-directed mutagenesis of the Wolinella succinogenes fumarate reductase operon. Eur J Biochem 251 : 418 426.
    • (1998) Eur J Biochem , vol.251 , pp. 418-426
    • Simon, J.1    Gross, R.2    Ringel, M.3    Schmidt, E.4    Kröger, A.5
  • 29
    • 0037014651 scopus 로고    scopus 로고
    • Modification of heme c binding motifs in the small subunit (NrfH) of the Wolinella succinogenes cytochrome c nitrite reductase complex
    • Simon, J., Eichler, R., Pisa, R., Biel, S. Gross, R. (2002) Modification of heme c binding motifs in the small subunit (NrfH) of the Wolinella succinogenes cytochrome c nitrite reductase complex. FEBS Lett 522 : 83 87.
    • (2002) FEBS Lett , vol.522 , pp. 83-87
    • Simon, J.1    Eichler, R.2    Pisa, R.3    Biel, S.4    Gross, R.5
  • 31
    • 11244338080 scopus 로고    scopus 로고
    • C-type cytochrome formation: Chemical and biological enigmas
    • Stevens, J.M., Daltrop, O., Allen, J.W.A. Ferguson, S.J. (2004) C-type cytochrome formation: chemical and biological enigmas. Acc Chem Res 37 : 999 1007.
    • (2004) Acc Chem Res , vol.37 , pp. 999-1007
    • Stevens, J.M.1    Daltrop, O.2    Allen, J.W.A.3    Ferguson, S.J.4
  • 32
    • 0037990786 scopus 로고    scopus 로고
    • Biogenesis of respiratory cytochromes in bacteria
    • Thöny-Meyer, L. (1997) Biogenesis of respiratory cytochromes in bacteria. Microbiol Mol Biol Rev 61 : 337 376.
    • (1997) Microbiol Mol Biol Rev , vol.61 , pp. 337-376
    • Thöny-Meyer, L.1
  • 33
    • 1842538862 scopus 로고    scopus 로고
    • Biochemical and spectroscopic characterization of the covalent binding of heme to cytochrome b6
    • de Vitry, C., Desbois, A., Redeker, V., Zito, F. Wollman, F.-A. (2004) Biochemical and spectroscopic characterization of the covalent binding of heme to cytochrome b6. Biochemistry 43 : 3956 3968.
    • (2004) Biochemistry , vol.43 , pp. 3956-3968
    • De Vitry, C.1    Desbois, A.2    Redeker, V.3    Zito, F.4    Wollman, F.-A.5
  • 34
    • 0033464509 scopus 로고    scopus 로고
    • Magnetic spectroscopic (EPR, ESEEM, Mössbauer, MCD and NMR) studies of low-spin ferriheme centers and their corresponding heme proteins
    • Walker, F.A. (1999) Magnetic spectroscopic (EPR, ESEEM, Mössbauer, MCD and NMR) studies of low-spin ferriheme centers and their corresponding heme proteins. Coord Chem Rev 186 : 471 534.
    • (1999) Coord Chem Rev , vol.186 , pp. 471-534
    • Walker, F.A.1
  • 35
    • 33845373654 scopus 로고
    • Models of the cytochromes b. Effect of axial ligand plane orientation on the EPR and Mössbauer spectra of low-spin ferrihemes
    • Walker, F.A., Huynh, B.H., Scheidt, W.R. Osvath, S.R. (1986) Models of the cytochromes b. Effect of axial ligand plane orientation on the EPR and Mössbauer spectra of low-spin ferrihemes. J Am Chem Soc 108 : 5288 5297.
    • (1986) J Am Chem Soc , vol.108 , pp. 5288-5297
    • Walker, F.A.1    Huynh, B.H.2    Scheidt, W.R.3    Osvath, S.R.4
  • 36
    • 0021101958 scopus 로고
    • Why do c-type cytochromes exist?
    • Wood, P.M. (1983) Why do c-type cytochromes exist? FEBS Lett 164 : 223 226.
    • (1983) FEBS Lett , vol.164 , pp. 223-226
    • Wood, P.M.1
  • 37
    • 0025905797 scopus 로고
    • Why do c-type cytochromes exist? Reprise
    • Wood, P.M. (1991) Why do c-type cytochromes exist? Reprise. Biochim Biophys Acta 1058 : 5 7.
    • (1991) Biochim Biophys Acta , vol.1058 , pp. 5-7
    • Wood, P.M.1
  • 38
    • 20844448190 scopus 로고    scopus 로고
    • Characterization of purified c-type heme-containing peptides and identification of c-type heme-attachment sites in Shewanella oneidensis cytochromes using mass spectrometry
    • Yang, F., Bogdanov, B., Strittmatter, E.F., Vilkov, A.N., Gritsenko, M., Shi, L., et al. (2005) Characterization of purified c-type heme-containing peptides and identification of c-type heme-attachment sites in Shewanella oneidensis cytochromes using mass spectrometry. J Proteome Res 4 : 846 854.
    • (2005) J Proteome Res , vol.4 , pp. 846-854
    • Yang, F.1    Bogdanov, B.2    Strittmatter, E.F.3    Vilkov, A.N.4    Gritsenko, M.5    Shi, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.