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Volumn 1777, Issue 7-8, 2008, Pages 980-984

Cytochrome c assembly: A tale of ever increasing variation and mystery?

Author keywords

c type cytochrome; Ccm system; Heme; Periplasm; Post translational modification; Thioether bond formation

Indexed keywords

CYTOCHROME C; ENZYME; HEME LYASE; SULFIDE;

EID: 46349106802     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2008.03.020     Document Type: Review
Times cited : (51)

References (45)
  • 1
    • 34248342168 scopus 로고    scopus 로고
    • A dedicated haem lyase is required for the maturation of a novel bacterial cytochrome c with unconventional covalent haem binding
    • Hartshorne R.S., Kern M., Meyer B., Clarke T.A., Karas M., Richardson D.J., and Simon J. A dedicated haem lyase is required for the maturation of a novel bacterial cytochrome c with unconventional covalent haem binding. Mol. Microbiol. 64 (2007) 1049-1060
    • (2007) Mol. Microbiol. , vol.64 , pp. 1049-1060
    • Hartshorne, R.S.1    Kern, M.2    Meyer, B.3    Clarke, T.A.4    Karas, M.5    Richardson, D.J.6    Simon, J.7
  • 2
    • 11244338080 scopus 로고    scopus 로고
    • C-type cytochrome formation: chemical and biological enigmas
    • Stevens J.M., Daltrop O., Allen J.W., and Ferguson S.J. C-type cytochrome formation: chemical and biological enigmas. Acc. Chem. Res. 37 (2004) 999-1007
    • (2004) Acc. Chem. Res. , vol.37 , pp. 999-1007
    • Stevens, J.M.1    Daltrop, O.2    Allen, J.W.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., Ginger M.L., and Ferguson S.J. Maturation of the unusual single-cysteine (XXXCH) mitochondrial c-type cytochromes found in trypanosomatids must occur through a novel biogenesis pathway. Biochem. J. 383 (2004) 537-542
    • (2004) Biochem. J. , vol.383 , pp. 537-542
    • Allen, J.W.1    Ginger, M.L.2    Ferguson, S.J.3
  • 4
    • 0344497439 scopus 로고    scopus 로고
    • An atypical haem in the cytochrome b(6)f complex
    • Stroebel D., Choquet Y., Popot J.L., and Picot D. An atypical haem in the cytochrome b(6)f complex. Nature 426 (2003) 413-418
    • (2003) Nature , vol.426 , pp. 413-418
    • Stroebel, D.1    Choquet, Y.2    Popot, J.L.3    Picot, D.4
  • 5
    • 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
  • 7
    • 8544284146 scopus 로고    scopus 로고
    • In vitro studies on thioether bond formation between Hydrogenobacter thermophilus apocytochrome c(552) with metalloprotoporphyrin derivatives
    • Daltrop O., and Ferguson S.J. In vitro studies on thioether bond formation between Hydrogenobacter thermophilus apocytochrome c(552) with metalloprotoporphyrin derivatives. J. Biol. Chem. 279 (2004) 45347-45353
    • (2004) J. Biol. Chem. , vol.279 , pp. 45347-45353
    • Daltrop, O.1    Ferguson, S.J.2
  • 8
    • 37549048614 scopus 로고    scopus 로고
    • Tuning the formation of a covalent haem-protein link by selection of reductive or oxidative conditions as exemplified by ascorbate peroxidase
    • Metcalfe C.L., Daltrop O., Ferguson S.J., and Raven E.L. Tuning the formation of a covalent haem-protein link by selection of reductive or oxidative conditions as exemplified by ascorbate peroxidase. Biochem. J. 408 (2007) 355-361
    • (2007) Biochem. J. , vol.408 , pp. 355-361
    • Metcalfe, C.L.1    Daltrop, O.2    Ferguson, S.J.3    Raven, E.L.4
  • 9
    • 0037471690 scopus 로고    scopus 로고
    • C-type cytochromes: diverse structures and biogenesis systems pose evolutionary problems
    • Allen J.W., Daltrop O., Stevens J.M., and Ferguson S.J. C-type cytochromes: diverse structures and biogenesis systems pose evolutionary problems. Phil. Trans. R. Soc. Lond. 358 (2003) 255-266
    • (2003) Phil. Trans. R. Soc. Lond. , vol.358 , pp. 255-266
    • Allen, J.W.1    Daltrop, O.2    Stevens, J.M.3    Ferguson, S.J.4
  • 10
    • 0346118951 scopus 로고    scopus 로고
    • Overlapping specificities of the mitochondrial cytochrome c and c1 heme lyases
    • Bernard D.G., Gabilly S.T., Dujardin G., Merchant S., and Hamel P.P. Overlapping specificities of the mitochondrial cytochrome c and c1 heme lyases. J. Biol. Chem. 278 (2003) 49732-49742
    • (2003) J. Biol. Chem. , vol.278 , pp. 49732-49742
    • Bernard, D.G.1    Gabilly, S.T.2    Dujardin, G.3    Merchant, S.4    Hamel, P.P.5
  • 11
    • 0032574759 scopus 로고    scopus 로고
    • Bacterial expression of a mitochondrial cytochrome c. Trimethylation of lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition
    • Pollock W.B., Rosell F.I., Twitchett M.B., Dumont M.E., and Mauk A.G. Bacterial expression of a mitochondrial cytochrome c. Trimethylation of lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition. Biochemistry 37 (1998) 6124-6131
    • (1998) Biochemistry , vol.37 , pp. 6124-6131
    • Pollock, W.B.1    Rosell, F.I.2    Twitchett, M.B.3    Dumont, M.E.4    Mauk, A.G.5
  • 12
    • 41449099521 scopus 로고    scopus 로고
    • The Erv1-Mia40 disulfide relay system in the intermembrane space of mitochondria
    • Hell K. The Erv1-Mia40 disulfide relay system in the intermembrane space of mitochondria. Biochim. Biophys. Acta 1783 (2008) 601-609
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 601-609
    • Hell, K.1
  • 13
    • 28844471305 scopus 로고    scopus 로고
    • Cyc2p, a membrane-bound flavoprotein involved in the maturation of mitochondrial c-type cytochromes
    • Bernard D.G., Quevillon-Cheruel S., Merchant S., Guiard B., and Hamel P.P. Cyc2p, a membrane-bound flavoprotein involved in the maturation of mitochondrial c-type cytochromes. J. Biol. Chem. 280 (2005) 39852-39859
    • (2005) J. Biol. Chem. , vol.280 , pp. 39852-39859
    • Bernard, D.G.1    Quevillon-Cheruel, S.2    Merchant, S.3    Guiard, B.4    Hamel, P.P.5
  • 14
    • 0036156055 scopus 로고    scopus 로고
    • Genomic analyses of bacterial respiratory and cytochrome c assembly systems: Bordetella as a model for the System II cytochrome c biogenesis pathway
    • Kranz R.G., Beckett C.S., and Goldman B.S. Genomic analyses of bacterial respiratory and cytochrome c assembly systems: Bordetella as a model for the System II cytochrome c biogenesis pathway. Res. Microbiol. 153 (2002) 1-6
    • (2002) Res. Microbiol. , vol.153 , pp. 1-6
    • Kranz, R.G.1    Beckett, C.S.2    Goldman, B.S.3
  • 15
    • 0036175133 scopus 로고    scopus 로고
    • Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can suppress cytochrome c deficiency of CcdA-defective Bacillus subtilis cells
    • Erlendsson L.S., and Hederstedt L. Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can suppress cytochrome c deficiency of CcdA-defective Bacillus subtilis cells. J. Bacteriol. 184 (2002) 1423-1429
    • (2002) J. Bacteriol. , vol.184 , pp. 1423-1429
    • Erlendsson, L.S.1    Hederstedt, L.2
  • 16
    • 33748053969 scopus 로고    scopus 로고
    • The housekeeping dipeptide permease is the Escherichia coli heme transporter and functions with two optional peptide binding proteins
    • Letoffe S., Delepelaire P., and Wandersman C. The housekeeping dipeptide permease is the Escherichia coli heme transporter and functions with two optional peptide binding proteins. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 12891-12896
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 12891-12896
    • Letoffe, S.1    Delepelaire, P.2    Wandersman, C.3
  • 18
    • 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., and Kranz R.G. Recombinant cytochromes c biogenesis systems I and II and analysis of haem delivery pathways in Escherichia coli. Mol. Microbiol. 60 (2006) 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
  • 19
    • 0037990786 scopus 로고    scopus 로고
    • Biogenesis of respiratory cytochromes in bacteria
    • Thony-Meyer L. Biogenesis of respiratory cytochromes in bacteria. Microbiol. Mol. Biol. Rev. 61 (1997) 337-376
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 337-376
    • Thony-Meyer, L.1
  • 22
    • 0032555539 scopus 로고    scopus 로고
    • Prototype of a heme chaperone essential for cytochrome c maturation
    • Schulz H., Hennecke H., and Thony-Meyer L. Prototype of a heme chaperone essential for cytochrome c maturation. Science 281 (1998) 1197-1200
    • (1998) Science , vol.281 , pp. 1197-1200
    • Schulz, H.1    Hennecke, H.2    Thony-Meyer, L.3
  • 23
    • 0038081179 scopus 로고    scopus 로고
    • Interaction of heme with variants of the heme chaperone CcmE carrying active site mutations and a cleavable N-terminal His tag
    • Stevens J.M., Daltrop O., Higham C.W., and Ferguson S.J. Interaction of heme with variants of the heme chaperone CcmE carrying active site mutations and a cleavable N-terminal His tag. J. Biol. Chem. 278 (2003) 20500-20506
    • (2003) J. Biol. Chem. , vol.278 , pp. 20500-20506
    • Stevens, J.M.1    Daltrop, O.2    Higham, C.W.3    Ferguson, S.J.4
  • 24
    • 0032529951 scopus 로고    scopus 로고
    • The CcmE protein from Escherichia coli is a haem-binding protein
    • Reid E., Eaves D.J., and Cole J.A. The CcmE protein from Escherichia coli is a haem-binding protein. FEMS Microbiol. Lett. 166 (1998) 369-375
    • (1998) FEMS Microbiol. Lett. , vol.166 , pp. 369-375
    • Reid, E.1    Eaves, D.J.2    Cole, J.A.3
  • 25
    • 34247398255 scopus 로고    scopus 로고
    • Loss of ATP hydrolysis activity by CcmAB results in loss of c-type cytochrome synthesis and incomplete processing of CcmE
    • Christensen O., Harvat E.M., Thony-Meyer L., Ferguson S.J., and Stevens J.M. Loss of ATP hydrolysis activity by CcmAB results in loss of c-type cytochrome synthesis and incomplete processing of CcmE. FEBS. 274 (2007) 2322-2332
    • (2007) FEBS. , vol.274 , pp. 2322-2332
    • Christensen, O.1    Harvat, E.M.2    Thony-Meyer, L.3    Ferguson, S.J.4    Stevens, J.M.5
  • 26
    • 33745224747 scopus 로고    scopus 로고
    • ABC transporter-mediated release of a haem chaperone allows cytochrome c biogenesis
    • Feissner R.E., Richard-Fogal C.L., Frawley E.R., and Kranz R.G. ABC transporter-mediated release of a haem chaperone allows cytochrome c biogenesis. Mol. Microbiol. 61 (2006) 219-231
    • (2006) Mol. Microbiol. , vol.61 , pp. 219-231
    • Feissner, R.E.1    Richard-Fogal, C.L.2    Frawley, E.R.3    Kranz, R.G.4
  • 27
    • 0037162447 scopus 로고    scopus 로고
    • The CcmE protein of the c-type cytochrome biogenesis system: unusual in vitro heme incorporation into apo-CcmE and transfer from holo-CcmE to apocytochrome
    • Daltrop O., Stevens J.M., Higham C.W., and Ferguson S.J. The CcmE protein of the c-type cytochrome biogenesis system: unusual in vitro heme incorporation into apo-CcmE and transfer from holo-CcmE to apocytochrome. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 9703-9708
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 9703-9708
    • Daltrop, O.1    Stevens, J.M.2    Higham, C.W.3    Ferguson, S.J.4
  • 28
    • 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., Griffiths I., and Cole J.A. 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 (1998) 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    Griffiths, I.7    Cole, J.A.8
  • 30
    • 0035311005 scopus 로고    scopus 로고
    • The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly
    • Reid E., Cole J., and Eaves D.J. The Escherichia coli CcmG protein fulfils a specific role in cytochrome c assembly. Biochem. J. 355 (2001) 51-58
    • (2001) Biochem. J. , vol.355 , pp. 51-58
    • Reid, E.1    Cole, J.2    Eaves, D.J.3
  • 32
    • 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., Griffiths I., and Cole J.A. 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 (1998) 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    Griffiths, I.7    Cole, J.A.8
  • 33
    • 0031919407 scopus 로고    scopus 로고
    • The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo
    • Fabianek R.A., Hennecke H., and Thony-Meyer L. The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo. J. Bacteriology 180 (1998) 1947-1950
    • (1998) J. Bacteriology , vol.180 , pp. 1947-1950
    • Fabianek, R.A.1    Hennecke, H.2    Thony-Meyer, L.3
  • 34
    • 38549150882 scopus 로고    scopus 로고
    • TPR domain of NrfG mediates complex formation between heme lyase and formate-dependent nitrite reductase in Escherichia coli O157:H7
    • Han D., Kim K., Oh J., Park J., and Kim Y. TPR domain of NrfG mediates complex formation between heme lyase and formate-dependent nitrite reductase in Escherichia coli O157:H7. Proteins 70 (2007) 900-914
    • (2007) Proteins , vol.70 , pp. 900-914
    • Han, D.1    Kim, K.2    Oh, J.3    Park, J.4    Kim, Y.5
  • 35
    • 4444368232 scopus 로고    scopus 로고
    • Biosynthesis of artificial microperoxidases by exploiting the secretion and cytochrome c maturation apparatuses of Escherichia coli
    • Braun M., and Thony-Meyer L. Biosynthesis of artificial microperoxidases by exploiting the secretion and cytochrome c maturation apparatuses of Escherichia coli. Proc. Natl. Acad. Sci. U. A. 101 (2004) 12830-12835
    • (2004) Proc. Natl. Acad. Sci. U. A. , vol.101 , pp. 12830-12835
    • Braun, M.1    Thony-Meyer, L.2
  • 36
    • 0028912363 scopus 로고
    • 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., and Ferguson S.J. 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. Mol. Microbiol. 15 (1995) 307-318
    • (1995) Mol. Microbiol. , vol.15 , pp. 307-318
    • Page, M.D.1    Ferguson, S.J.2
  • 37
    • 20444437622 scopus 로고    scopus 로고
    • Overproduction of CcmG and CcmFH(Rc) fully suppresses the c-type cytochrome biogenesis defect of Rhodobacter capsulatus CcmI-null mutants
    • Sanders C., Deshmukh M., Astor D., Kranz R.G., and Daldal F. Overproduction of CcmG and CcmFH(Rc) fully suppresses the c-type cytochrome biogenesis defect of Rhodobacter capsulatus CcmI-null mutants. J. Bacteriol. 187 (2005) 4245-4256
    • (2005) J. Bacteriol. , vol.187 , pp. 4245-4256
    • Sanders, C.1    Deshmukh, M.2    Astor, D.3    Kranz, R.G.4    Daldal, F.5
  • 38
    • 33846583327 scopus 로고    scopus 로고
    • Membrane-spanning and periplasmic segments of CcmI have distinct functions during cytochrome c biogenesis in Rhodobacter capsulatus
    • Sanders C., Boulay C., and Daldal F. Membrane-spanning and periplasmic segments of CcmI have distinct functions during cytochrome c biogenesis in Rhodobacter capsulatus. J. Bacteriol. 189 (2007) 789-800
    • (2007) J. Bacteriol. , vol.189 , pp. 789-800
    • Sanders, C.1    Boulay, C.2    Daldal, F.3
  • 39
    • 33747834407 scopus 로고    scopus 로고
    • A variant System I for cytochrome c biogenesis in archaea and some bacteria has a novel CcmE and no CcmH
    • Allen J.W., Harvat E.M., Stevens J.M., and Ferguson S.J. A variant System I for cytochrome c biogenesis in archaea and some bacteria has a novel CcmE and no CcmH. FEBS Lett. 580 (2006) 4827-4834
    • (2006) FEBS Lett. , vol.580 , pp. 4827-4834
    • Allen, J.W.1    Harvat, E.M.2    Stevens, J.M.3    Ferguson, S.J.4
  • 41
    • 0035980054 scopus 로고    scopus 로고
    • Physical interaction of CcmC with heme and the heme chaperone CcmE during cytochrome c maturation
    • Ren Q., and Thony-Meyer L. Physical interaction of CcmC with heme and the heme chaperone CcmE during cytochrome c maturation. J. Biol. Chem. 276 (2001) 32591-32596
    • (2001) J. Biol. Chem. , vol.276 , pp. 32591-32596
    • Ren, Q.1    Thony-Meyer, L.2
  • 42
    • 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., and Ferguson S.J. 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 (2002) 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
  • 44
    • 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., and Gross R. Modification of heme c binding motifs in the small subunit (NrfH) of the Wolinella succinogenes cytochrome c nitrite reductase complex. FEBS Lett. 522 (2002) 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
  • 45
    • 34547407925 scopus 로고    scopus 로고
    • A specific c-type cytochrome maturation system is required for oxygenic photosynthesis
    • Kuras R., Saint-Marcoux D., Wollman F.A., and de Vitry C. A specific c-type cytochrome maturation system is required for oxygenic photosynthesis. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 9906-9910
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 9906-9910
    • Kuras, R.1    Saint-Marcoux, D.2    Wollman, F.A.3    de Vitry, C.4


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