메뉴 건너뛰기




Volumn 278, Issue 22, 2011, Pages 4189-4197

Cytochrome c maturation system on the negative side of bioenergetic membranes: CCB or System IV

Author keywords

biogenesis; c type cytochrome; chloroplast; heme; photosynthesis

Indexed keywords

CYTOCHROME C; CYTOCHROME C MATURATION 1; CYTOCHROME C MATURATION 2; CYTOCHROME C MATURATION 3; CYTOCHROME C MATURATION 4; CYTOCHROME C MATURATION SYSTEM IV; HEME; MICROORGANISM PROTEIN; SULFIDE; UNCLASSIFIED DRUG;

EID: 80255136293     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08373.x     Document Type: Review
Times cited : (33)

References (62)
  • 2
    • 31544467296 scopus 로고    scopus 로고
    • Cytochrome c: Occurrence and functions
    • DOI 10.1021/cr050241v
    • Bertini I, Cavallaro G, &, Rosato A, (2006) Cytochrome c: occurrence and functions. Chem Rev 106, 90-115. (Pubitemid 43159622)
    • (2006) Chemical Reviews , vol.106 , Issue.1 , pp. 90-115
    • Bertini, I.1    Cavallaro, G.2    Rosato, A.3
  • 3
  • 4
    • 0031875674 scopus 로고    scopus 로고
    • Molecular mechanisms of cytochrome c biogenesis: Three distinct systems
    • DOI 10.1046/j.1365-2958.1998.00869.x
    • 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. (Pubitemid 28330775)
    • (1998) Molecular Microbiology , vol.29 , Issue.2 , pp. 383-396
    • Kranz, R.1    Lill, R.2    Goldman, B.3    Bonnard, G.4    Merchant, S.5
  • 5
    • 58949093219 scopus 로고    scopus 로고
    • The chemistry and biochemistry of heme c: Functional bases for covalent attachment
    • Bowman SE, &, Bren KL, (2008) The chemistry and biochemistry of heme c: functional bases for covalent attachment. Nat Prod Rep 25, 1118-1130.
    • (2008) Nat Prod Rep , vol.25 , pp. 1118-1130
    • Bowman, S.E.1    Bren, K.L.2
  • 9
    • 70349309436 scopus 로고    scopus 로고
    • Cytochrome c biogenesis: Mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control
    • Kranz RG, Richard-Fogal C, Taylor JS, &, Frawley ER, (2009) Cytochrome c biogenesis: mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control. Microbiol Mol Biol Rev 73, 510-528.
    • (2009) Microbiol Mol Biol Rev , vol.73 , pp. 510-528
    • Kranz, R.G.1    Richard-Fogal, C.2    Taylor, J.S.3    Frawley, E.R.4
  • 10
    • 80255137210 scopus 로고    scopus 로고
    • Composition and function of cytochrome c biogenesis System II
    • Simon J, &, Hederstedt L, (2011) Composition and function of cytochrome c biogenesis System II. FEBS J 278, 4179-4188.
    • (2011) FEBS J , vol.278 , pp. 4179-4188
    • Simon, J.1    Hederstedt, L.2
  • 13
    • 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
    • DOI 10.1042/BJ20040832
    • Allen JW, Ginger ML, &, Ferguson SJ, (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. (Pubitemid 39546124)
    • (2004) Biochemical Journal , vol.383 , Issue.3 , pp. 537-542
    • Allen, J.W.A.1    Ginger, M.L.2    Ferguson, S.J.3
  • 14
    • 65349186331 scopus 로고    scopus 로고
    • Structure of a trypanosomatid mitochondrial cytochrome c with heme attached via only one thioether bond and implications for the substrate recognition requirements of heme lyase
    • Fulop V, Sam KA, Ferguson SJ, Ginger ML, &, Allen JW, (2009) Structure of a trypanosomatid mitochondrial cytochrome c with heme attached via only one thioether bond and implications for the substrate recognition requirements of heme lyase. FEBS J 276, 2822-2832.
    • (2009) FEBS J , vol.276 , pp. 2822-2832
    • Fulop, V.1    Sam, K.A.2    Ferguson, S.J.3    Ginger, M.L.4    Allen, J.W.5
  • 15
    • 0016754421 scopus 로고
    • The protonmotive Q cycle: A general formulation
    • Mitchell P, (1975) The protonmotive Q cycle: a general formulation. FEBS Lett 59, 137-139.
    • (1975) FEBS Lett , vol.59 , pp. 137-139
    • Mitchell, P.1
  • 16
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • Mitchell P, (1976) Possible molecular mechanisms of the protonmotive function of cytochrome systems. J Theor Biol 62, 327-367.
    • (1976) J Theor Biol , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 17
    • 0020173148 scopus 로고
    • A Q-cycle mechanism for the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides
    • Crofts AR, &, Meinhardt SW, (1982) A Q-cycle mechanism for the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides. Biochem Soc Trans 10, 201-203.
    • (1982) Biochem Soc Trans , vol.10 , pp. 201-203
    • Crofts, A.R.1    Meinhardt, S.W.2
  • 18
    • 0344497439 scopus 로고    scopus 로고
    • 6f complex
    • DOI 10.1038/nature02155
    • Stroebel D, Choquet Y, Popot JL, &, Picot D, (2003) An atypical haem in the cytochrome b(6)f complex. Nature 426, 413-418. (Pubitemid 37490123)
    • (2003) Nature , vol.426 , Issue.6965 , pp. 413-418
    • Stroebel, D.1    Choquet, Y.2    Popot, J.-L.3    Picot, D.4
  • 19
    • 0242494128 scopus 로고    scopus 로고
    • 6f Complex of Oxygenic Photosynthesis: Tuning the Cavity
    • DOI 10.1126/science.1090165
    • 6f complex of oxygenic photosynthesis: tuning the cavity. Science 302, 1009-1014. (Pubitemid 37386186)
    • (2003) Science , vol.302 , Issue.5647 , pp. 1009-1014
    • Kurisu, G.1    Zhang, H.2    Smith, J.L.3    Cramer, W.A.4
  • 22
    • 0002565747 scopus 로고
    • Membrane potential-dependant reduction of cytochrome b-6 in an algal mutant lacking photosystem i centers
    • Lavergne J, (1983) Membrane potential-dependant reduction of cytochrome b-6 in an algal mutant lacking photosystem I centers. Biochim Biophys Acta 725, 25-33.
    • (1983) Biochim Biophys Acta , vol.725 , pp. 25-33
    • Lavergne, J.1
  • 23
    • 0001695270 scopus 로고
    • The low-potential electron transfer chain in the cytochrome b/f complex
    • Joliot P, &, Joliot A, (1988) The low-potential electron transfer chain in the cytochrome b/f complex. Biochim Biophys Acta 933, 319-333.
    • (1988) Biochim Biophys Acta , vol.933 , pp. 319-333
    • Joliot, P.1    Joliot, A.2
  • 27
    • 77953649544 scopus 로고    scopus 로고
    • Heliobacterial Rieske/cytb complex
    • Baymann F, &, Nitschke W, (2010) Heliobacterial Rieske/cytb complex. Photosynth Res 104, 177-187.
    • (2010) Photosynth Res , vol.104 , pp. 177-187
    • Baymann, F.1    Nitschke, W.2
  • 31
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson O, Nielsen H, &, von Heijne G, (1999) ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci 8, 978-984. (Pubitemid 29211735)
    • (1999) Protein Science , vol.8 , Issue.5 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 32
    • 0028279520 scopus 로고
    • Prediction of transmembrane segments in proteins utilising multiple sequence alignments
    • DOI 10.1006/jmbi.1994.1220
    • Persson B, &, Argos P, (1994) Prediction of transmembrane segments in proteins utilising multiple sequence alignments. J Mol Biol 237, 182-192. (Pubitemid 24182232)
    • (1994) Journal of Molecular Biology , vol.237 , Issue.2 , pp. 182-192
    • Persson, B.1    Argos, P.2
  • 33
    • 0025896455 scopus 로고
    • The 'positive-inside rule' applies to thylakoid membrane proteins
    • Gavel Y, Steppuhn J, Herrmann R, &, von Heijne G, (1991) The 'positive-inside rule' applies to thylakoid membrane proteins. FEBS Lett 282, 41-46.
    • (1991) FEBS Lett , vol.282 , pp. 41-46
    • Gavel, Y.1    Steppuhn, J.2    Herrmann, R.3    Von Heijne, G.4
  • 35
    • 0035965335 scopus 로고    scopus 로고
    • Insertion of PsaK into the thylakoid membrane in a 'Horseshoe' conformation occurs in the absence of signal recognition particle, nucleoside triphosphates, or functional albino3
    • Mant A, Woolhead CA, Moore M, Henry R, &, Robinson C, (2001) Insertion of PsaK into the thylakoid membrane in a 'Horseshoe' conformation occurs in the absence of signal recognition particle, nucleoside triphosphates, or functional albino3. J Biol Chem 276, 36200-36206.
    • (2001) J Biol Chem , vol.276 , pp. 36200-36206
    • Mant, A.1    Woolhead, C.A.2    Moore, M.3    Henry, R.4    Robinson, C.5
  • 36
    • 33744517666 scopus 로고    scopus 로고
    • The properties of the positively charged loop region in PSI-G are essential for its "spontaneous" insertion into thylakoids and rapid assembly into the photosystem I complex
    • DOI 10.1074/jbc.M512687200
    • Zygadlo A, Robinson C, Scheller HV, Mant A, &, Jensen PE, (2006) The properties of the positively charged loop region in PSI-G are essential for its 'spontaneous' insertion into thylakoids and rapid assembly into the photosystem I complex. J Biol Chem 281, 10548-10554. (Pubitemid 43864595)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.15 , pp. 10548-10554
    • Zygadlo, A.1    Robinson, C.2    Scheller, H.V.3    Mant, A.4    Jensen, P.E.5
  • 37
    • 0037462720 scopus 로고    scopus 로고
    • Essential histidine and tryptophan residues in CcsA, a system II polytopic cytochrome c biogenesis protein
    • DOI 10.1074/jbc.M208651200
    • Hamel PP, Dreyfuss BW, Xie Z, Gabilly ST, &, Merchant S, (2003) Essential histidine and tryptophan residues in CcsA, a system II polytopic cytochrome c biogenesis protein. J Biol Chem 278, 2593-2603. (Pubitemid 36801338)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.4 , pp. 2593-2603
    • Hamel, P.P.1    Dreyfuss, B.W.2    Xie, Z.3    Gabilly, S.T.4    Merchant, S.5
  • 38
    • 0032555539 scopus 로고    scopus 로고
    • Prototype of a heme chaperone essential for cytochrome c maturation
    • Schulz H, Hennecke H, &, Thony-Meyer L, (1998) Prototype of a heme chaperone essential for cytochrome c maturation. Science 281, 1197-1200. (Pubitemid 28406296)
    • (1998) Science , vol.281 , Issue.5380 , pp. 1197-1200
    • Schulz, H.1    Hennecke, H.2    Thony-Meyer, L.3
  • 39
    • 77957030496 scopus 로고    scopus 로고
    • Redox processes controlling the biogenesis of c-type cytochromes
    • Bonnard G, Corvest V, Meyer EH, &, Hamel PP, (2010) Redox processes controlling the biogenesis of c-type cytochromes. Antioxid Redox Signal 13, 1385-1401.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1385-1401
    • Bonnard, G.1    Corvest, V.2    Meyer, E.H.3    Hamel, P.P.4
  • 40
    • 0035209897 scopus 로고    scopus 로고
    • 6f complex in Arabidopsis
    • DOI 10.1105/tpc.13.11.2539
    • Lennartz K, Plucken H, Seidler A, Westhoff P, Bechtold N, &, Meierhoff K, (2001) HCF164 encodes a thioredoxin-like protein involved in the biogenesis of the cytochrome b(6)f complex in Arabidopsis. Plant Cell 13, 2539-2551. (Pubitemid 33146115)
    • (2001) Plant Cell , vol.13 , Issue.11 , pp. 2539-2551
    • Lennartz, K.1    Plucken, H.2    Seidler, A.3    Westhoff, P.4    Bechtold, N.5    Meierhoff, K.6
  • 41
    • 56349145181 scopus 로고    scopus 로고
    • Thiol oxidation in bacteria, mitochondria and chloroplasts: Common principles but three unrelated machineries?
    • Herrmann JM, Kauff F, &, Neuhaus HE, (2009) Thiol oxidation in bacteria, mitochondria and chloroplasts: common principles but three unrelated machineries? Biochim Biophys Acta 1793, 71-77.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 71-77
    • Herrmann, J.M.1    Kauff, F.2    Neuhaus, H.E.3
  • 42
    • 33644993357 scopus 로고    scopus 로고
    • Subcellular localization and light-regulated expression of protoporphyrinogen IX oxidase and ferrochelatase in Chlamydomonas reinhardtii
    • DOI 10.1104/pp.105.069732
    • van Lis R, Atteia A, Nogaj LA, &, Beale SI, (2005) Subcellular localization and light-regulated expression of protoporphyrinogen IX oxidase and ferrochelatase in Chlamydomonas reinhardtii. Plant Physiol 139, 1946-1958. (Pubitemid 43899830)
    • (2005) Plant Physiology , vol.139 , Issue.4 , pp. 1946-1958
    • Van Lis, R.1    Atteia, A.2    Nogaj, L.A.3    Beale, S.I.4
  • 45
    • 65249119677 scopus 로고    scopus 로고
    • Orthogenomics of photosynthetic organisms: Bioinformatic and experimental analysis of chloroplast proteins of endosymbiont origin in Arabidopsis and their counterparts in Synechocystis
    • Ishikawa M, Fujiwara M, Sonoike K, &, Sato N, (2009) Orthogenomics of photosynthetic organisms: bioinformatic and experimental analysis of chloroplast proteins of endosymbiont origin in Arabidopsis and their counterparts in Synechocystis. Plant Cell Physiol 50, 773-788.
    • (2009) Plant Cell Physiol , vol.50 , pp. 773-788
    • Ishikawa, M.1    Fujiwara, M.2    Sonoike, K.3    Sato, N.4
  • 47
    • 77950545784 scopus 로고    scopus 로고
    • The YlmG protein has a conserved function related to the distribution of nucleoids in chloroplasts and cyanobacteria
    • Kabeya Y, Nakanishi H, Suzuki K, Ichikawa T, Kondou Y, Matsui M, &, Miyagishima SY, (2010) The YlmG protein has a conserved function related to the distribution of nucleoids in chloroplasts and cyanobacteria. BMC Plant Biol 10, 57.
    • (2010) BMC Plant Biol , vol.10 , pp. 57
    • Kabeya, Y.1    Nakanishi, H.2    Suzuki, K.3    Ichikawa, T.4    Kondou, Y.5    Matsui, M.6    Miyagishima, S.Y.7
  • 51
    • 0024730745 scopus 로고
    • Posttranslational events leading to the assembly of photosystem II protein complex: A study using photosynthesis mutants from Chlamydomonas reinhardtii
    • de Vitry C, Olive J, Drapier D, Recouvreur M, &, Wollman FA, (1989) Posttranslational events leading to the assembly of photosystem II protein complex: a study using photosynthesis mutants from Chlamydomonas reinhardtii. J Cell Biol 109, 991-1006.
    • (1989) J Cell Biol , vol.109 , pp. 991-1006
    • De Vitry, C.1    Olive, J.2    Drapier, D.3    Recouvreur, M.4    Wollman, F.A.5
  • 52
    • 0031706227 scopus 로고    scopus 로고
    • Gene modifications and mutation mapping to study the function of photosystem II
    • DOI 10.1016/S0076-6879(98)97022-7
    • Vermaas WF, (1998) Gene modifications and mutation mapping to study the function of photosystem II. Methods Enzymol 297, 293-310. (Pubitemid 28449511)
    • (1998) Methods in Enzymology , vol.297 , pp. 293-310
    • Vermaas, W.F.J.1
  • 53
    • 0032910388 scopus 로고    scopus 로고
    • The biogenesis and assembly of photosynthetic proteins in thylakoid membranes
    • DOI 10.1016/S0005-2728(99)00043-2, PII S0005272899000432
    • Wollman FA, Minai L, &, Nechushtai R, (1999) The biogenesis and assembly of photosynthetic proteins in thylakoid membranes. Biochim Biophys Acta 1411, 21-85. (Pubitemid 29182797)
    • (1999) Biochimica et Biophysica Acta - Bioenergetics , vol.1411 , Issue.1 , pp. 21-85
    • Wollman, F.-A.1    Minai, L.2    Nechushtai, R.3
  • 54
    • 0021807837 scopus 로고
    • Gram-positive bacteria: possible photosynthetic ancestry
    • Woese CR, Debrunner-Vossbrinck BA, Oyaizu H, Stackebrandt E, &, Ludwig W, (1985) Gram-positive bacteria: possible photosynthetic ancestry. Science 229, 762-765. (Pubitemid 15049819)
    • (1985) Science , vol.229 , Issue.4715 , pp. 762-765
    • Woese, C.R.1    Debrunner-Vossbrinck, B.A.2    Oyaizu, H.3
  • 56
    • 0032502756 scopus 로고    scopus 로고
    • Studies of the cytochrome subunits of menaquinone: Cytochrome c reductase (bc complex) of Bacillus subtilis. Evidence for the covalent attachment of heme to the cytochrome b subunit
    • DOI 10.1074/jbc.273.15.8860
    • Yu J, &, Le Brun NE, (1998) Studies of the cytochrome subunits of menaquinone:cytochrome c reductase (bc complex) of Bacillus subtilis. Evidence for the covalent attachment of heme to the cytochrome b subunit. J Biol Chem 273, 8860-8866. (Pubitemid 28176167)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.15 , pp. 8860-8866
    • Yu, J.1    Le Brun, N.E.2
  • 58
    • 0141994961 scopus 로고    scopus 로고
    • Characterization of divIVA and other genes located in the chromosomal region downstream of the dcw cluster in Streptococcus pneumoniae
    • DOI 10.1128/JB.185.20.6209-6214.2003
    • Fadda D, Pischedda C, Caldara F, Whalen MB, Anderluzzi D, Domenici E, &, Massidda O, (2003) Characterization of divIVA and other genes located in the chromosomal region downstream of the dcw cluster in Streptococcus pneumoniae. J Bacteriol 185, 6209-6214. (Pubitemid 37248476)
    • (2003) Journal of Bacteriology , vol.185 , Issue.20 , pp. 6209-6214
    • Fadda, D.1    Pischedda, C.2    Caldara, F.3    Whalen, M.B.4    Anderluzzi, D.5    Domenici, E.6    Massidda, O.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.