메뉴 건너뛰기




Volumn 28, Issue 16, 2009, Pages 2349-2359

A conserved haem redox and trafficking pathway for cofactor attachment

Author keywords

Cytochrome; Haem; Quinone; Redox

Indexed keywords

CYTOCHROME B; CYTOCHROME C; HEME; IRON; QUINONE DERIVATIVE;

EID: 69249205419     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2009.189     Document Type: Article
Times cited : (56)

References (47)
  • 1
    • 0347993106 scopus 로고    scopus 로고
    • Dynamic features of a heme delivery system for cytochrome C maturation
    • Ahuja U, Thony-Meyer L (2003) Dynamic features of a heme delivery system for cytochrome C maturation. J Biol Chem 278: 52061-52070
    • (2003) J Biol Chem , vol.278 , pp. 52061-52070
    • Ahuja, U.1    Thony-Meyer, L.2
  • 4
    • 0033678963 scopus 로고    scopus 로고
    • Four genes are required for the system II cytochrome c biogenesis pathway in Bordetella pertussis, a unique bacterial model
    • Beckett CS, Loughman JA, Karberg KA, Donato GM, Goldman WE, Kranz RG (2000) Four genes are required for the system II cytochrome c biogenesis pathway in Bordetella pertussis, a unique bacterial model. Mol Microbiol 38: 465-481
    • (2000) Mol Microbiol , vol.38 , pp. 465-481
    • Beckett, C.S.1    Loughman, J.A.2    Karberg, K.A.3    Donato, G.M.4    Goldman, W.E.5    Kranz, R.G.6
  • 6
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • Berry EA, Trumpower BL (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
  • 7
    • 0036670802 scopus 로고    scopus 로고
    • Terminal steps of haem biosynthesis
    • Dailey HA (2002) Terminal steps of haem biosynthesis. Biochem Soc Trans 30: 590-595
    • (2002) Biochem Soc Trans , vol.30 , pp. 590-595
    • Dailey, H.A.1
  • 8
    • 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 JM, Higham CW, Ferguson SJ (2002) 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 USA 99: 9703-9708
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9703-9708
    • Daltrop, O.1    Stevens, J.M.2    Higham, C.W.3    Ferguson, S.J.4
  • 9
    • 0037214399 scopus 로고    scopus 로고
    • Biochemical and mutational characterization of the heme chaper-one CcmE reveals a heme binding site
    • Enggist E, Schneider MJ, Schulz H, Thony-Meyer L (2003) Biochemical and mutational characterization of the heme chaper-one CcmE reveals a heme binding site. J Bacteriol 185: 175-183
    • (2003) J Bacteriol , vol.185 , pp. 175-183
    • Enggist, E.1    Schneider, M.J.2    Schulz, H.3    Thony-Meyer, L.4
  • 10
    • 33745224747 scopus 로고    scopus 로고
    • ABC transporter-mediated release of a haem chaperone allows cytochrome c biogenesis
    • Feissner RE, Richard-Fogal CL, Frawley ER, Kranz RG (2006a) ABC transporter-mediated release of a haem chaperone allows cytochrome c biogenesis. Mol Microbiol 61: 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
  • 11
    • 33645809956 scopus 로고    scopus 로고
    • Recombinant cytochromes c biogenesis systems I and II and analysis of haem delivery pathways in Escherichia coli
    • Feissner RE, Richard-Fogal CL, Frawley ER, Loughman JA, Earley KW, Kranz RG (2006b) 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
  • 13
    • 67649878164 scopus 로고    scopus 로고
    • CcsBA is a cytochrome c synthetase that also functions in heme transport
    • Frawley ER, Kranz RG (2009) CcsBA is a cytochrome c synthetase that also functions in heme transport. Proc Natl Acad Sci USA 106: 10201-10206
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 10201-10206
    • Frawley, E.R.1    Kranz, R.G.2
  • 14
    • 33846813578 scopus 로고    scopus 로고
    • Axial coordination of heme in ferric CcmE chaperone characterized by EPR spectroscopy
    • Garcia-Rubio I, Braun M, Gromov I, Thony-Meyer L, Schweiger A (2007) Axial coordination of heme in ferric CcmE chaperone characterized by EPR spectroscopy. Biophys J 92: 1361-1373
    • (2007) Biophys J , vol.92 , pp. 1361-1373
    • Garcia-Rubio, I.1    Braun, M.2    Gromov, I.3    Thony-Meyer, L.4    Schweiger, A.5
  • 16
    • 56349110794 scopus 로고    scopus 로고
    • Biochemical requirements for the maturation of mitochondrial c-type cyto-chromes
    • Hamel P, Corvest V, Giege P, Bonnard G (2009) Biochemical requirements for the maturation of mitochondrial c-type cyto-chromes. Biochim Biophys Acta 1793: 125-138
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 125-138
    • Hamel, P.1    Corvest, V.2    Giege, P.3    Bonnard, G.4
  • 17
    • 34548137051 scopus 로고    scopus 로고
    • Intracellular trafficking of porphyrins
    • Hamza I (2006) Intracellular trafficking of porphyrins. ACS Chem Biol 1: 627-629
    • (2006) ACS Chem Biol , vol.1 , pp. 627-629
    • Hamza, I.1
  • 18
    • 64349090263 scopus 로고    scopus 로고
    • Probing the heme-binding site of the cytochrome c maturation protein CcmE
    • Harvat EM, Redfield C, Stevens JM, Ferguson SJ (2009) Probing the heme-binding site of the cytochrome c maturation protein CcmE. Biochemistry 48: 1820-1828
    • (2009) Biochemistry , vol.48 , pp. 1820-1828
    • Harvat, E.M.1    Redfield, C.2    Stevens, J.M.3    Ferguson, S.J.4
  • 20
    • 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
  • 23
    • 34548488226 scopus 로고    scopus 로고
    • Evolutionary origins of members of a superfamily of integral membrane cytochrome c biogenesis proteins
    • Lee JH, Harvat EM, Stevens JM, Ferguson SJ, Saier Jr MH (2007) Evolutionary origins of members of a superfamily of integral membrane cytochrome c biogenesis proteins. Biochim Biophys Acta 1768: 2164-2181
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 2164-2181
    • Lee, J.H.1    Harvat, E.M.2    Stevens, J.M.3    Ferguson, S.J.4    Saier Jr, M.H.5
  • 25
    • 0024408905 scopus 로고
    • Import of cytochrome c into mitochondria: Reduction of heme, mediated by NADH and flavin nucleotides, is obligatory for its covalent linkage to apocyto-chrome c
    • Nicholson DW, Neupert W (1989) Import of cytochrome c into mitochondria: reduction of heme, mediated by NADH and flavin nucleotides, is obligatory for its covalent linkage to apocyto-chrome c. Proc Natl Acad Sci USA 86: 4340-4344
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 4340-4344
    • Nicholson, D.W.1    Neupert, W.2
  • 26
    • 0035985617 scopus 로고    scopus 로고
    • Biochemistry, regulation and genomics of haem biosynthesis in prokaryotes
    • O'Brian MR, Thony-Meyer L (2002) Biochemistry, regulation and genomics of haem biosynthesis in prokaryotes. Adv Microb Physiol 46: 257-318
    • (2002) Adv Microb Physiol , vol.46 , pp. 257-318
    • O'Brian, M.R.1    Thony-Meyer, L.2
  • 28
    • 1542274585 scopus 로고    scopus 로고
    • 562 of the Saccharomyces cerevisiae succinate dehydrogenase
    • 562 of the Saccharomyces cerevisiae succinate dehydrogenase. J Biol Chem 279: 9432-9439
    • (2004) J Biol Chem , vol.279 , pp. 9432-9439
    • Oyedotun, K.S.1    Yau, P.F.2    Lemire, B.D.3
  • 29
    • 0033104207 scopus 로고    scopus 로고
    • A colorimetric assay for heme in biological samples using 96-well plates
    • Pandey AV, Joshi SK, Tekwani BL, Chauhan VS (1999) A colorimetric assay for heme in biological samples using 96-well plates. Anal Biochem 268: 159-161
    • (1999) Anal Biochem , vol.268 , pp. 159-161
    • Pandey, A.V.1    Joshi, S.K.2    Tekwani, B.L.3    Chauhan, V.S.4
  • 32
    • 0041935939 scopus 로고    scopus 로고
    • National Institutes of Health: Bethesda, MD
    • Rasband W (1997-2008) ImageJ. National Institutes of Health: Bethesda, MD
    • (1997) ImageJ
    • Rasband, W.1
  • 33
    • 54449100867 scopus 로고    scopus 로고
    • The three mitochondrial encoded CcmF proteins form a complex that interacts with CCMH and c-type apocytochromes in Arabidopsis
    • Rayapuram N, Hagenmuller J, Grienenberger JM, Bonnard G, Giege P (2008) The three mitochondrial encoded CcmF proteins form a complex that interacts with CCMH and c-type apocytochromes in Arabidopsis. J Biol Chem 283: 25200-25208
    • (2008) J Biol Chem , vol.283 , pp. 25200-25208
    • Rayapuram, N.1    Hagenmuller, J.2    Grienenberger, J.M.3    Bonnard, G.4    Giege, P.5
  • 34
    • 0037040888 scopus 로고    scopus 로고
    • A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c
    • Ren Q, Ahuja U, Thony-Meyer L (2002) A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c. J Biol Chem 277: 7657-7663
    • (2002) J Biol Chem , vol.277 , pp. 7657-7663
    • Ren, Q.1    Ahuja, U.2    Thony-Meyer, L.3
  • 35
    • 0035980054 scopus 로고    scopus 로고
    • Physical interaction of CcmC with heme and the heme chaperone CcmE during cytochrome c maturation
    • Ren Q, Thony-Meyer L (2001) Physical interaction of CcmC with heme and the heme chaperone CcmE during cytochrome c maturation. J Biol Chem 276: 32591-32596
    • (2001) J Biol Chem , vol.276 , pp. 32591-32596
    • Ren, Q.1    Thony-Meyer, L.2
  • 36
    • 33846234254 scopus 로고    scopus 로고
    • Heme concentration dependence and metalloporphyrin inhibition of the system I and II cytochrome c assembly pathways
    • Richard-Fogal CL, Frawley ER, Feissner RE, Kranz RG (2007) Heme concentration dependence and metalloporphyrin inhibition of the system I and II cytochrome c assembly pathways. J Bacteriol 189: 455-463
    • (2007) J Bacteriol , vol.189 , pp. 455-463
    • Richard-Fogal, C.L.1    Frawley, E.R.2    Feissner, R.E.3    Kranz, R.G.4
  • 37
    • 47049130022 scopus 로고    scopus 로고
    • Topology and function of CcmD in cytochrome c maturation
    • Richard-Fogal CL, Frawley ER, Kranz RG (2008) Topology and function of CcmD in cytochrome c maturation. J Bacteriol 190: 3489-3493
    • (2008) J Bacteriol , vol.190 , pp. 3489-3493
    • Richard-Fogal, C.L.1    Frawley, E.R.2    Kranz, R.G.3
  • 39
    • 57649165529 scopus 로고    scopus 로고
    • The cytochrome c maturation components CcmF, CcmH, and Ccml form a membrane-integral multisubunit heme ligation complex
    • Sanders C, Turkarslan S, Lee DW, Onder O, Kranz RG, Daldal F (2008) The cytochrome c maturation components CcmF, CcmH, and Ccml form a membrane-integral multisubunit heme ligation complex. J Biol Chem 283: 29715-29722
    • (2008) J Biol Chem , vol.283 , pp. 29715-29722
    • Sanders, C.1    Turkarslan, S.2    Lee, D.W.3    Onder, O.4    Kranz, R.G.5    Daldal, F.6
  • 40
    • 0033033305 scopus 로고    scopus 로고
    • Heme transfer to the heme chaperone CcmE during cytochrome c maturation requires the CcmC protein, which may function independently of the ABC-transporter CcmAB
    • Schulz H, Fabianek RA, Pellicioli EC, Hennecke H, Thony-Meyer L (1999) Heme transfer to the heme chaperone CcmE during cytochrome c maturation requires the CcmC protein, which may function independently of the ABC-transporter CcmAB. Proc Natl Acad Sci USA 96: 6462-6467
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6462-6467
    • Schulz, H.1    Fabianek, R.A.2    Pellicioli, E.C.3    Hennecke, H.4    Thony-Meyer, L.5
  • 41
    • 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
    • (1998) Science , vol.281 , pp. 1197-1200
    • Schulz, H.1    Hennecke, H.2    Thony-Meyer, L.3
  • 43
    • 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 JM, Daltrop O, Higham CW, Ferguson SJ (2003) 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: 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
  • 44
    • 33646594462 scopus 로고    scopus 로고
    • Identification of a ubiquinone-binding site that affects autophosphorylation of the sensor kinase RegB
    • Swem LR, Gong X, Yu CA, Bauer CE (2006) Identification of a ubiquinone-binding site that affects autophosphorylation of the sensor kinase RegB. J Biol Chem 281: 6768-6775
    • (2006) J Biol Chem , vol.281 , pp. 6768-6775
    • Swem, L.R.1    Gong, X.2    Yu, C.A.3    Bauer, C.E.4
  • 45
    • 0036671471 scopus 로고    scopus 로고
    • Cytochrome c maturation: A complex pathway for a simple task?
    • Thony-Meyer L (2002) Cytochrome c maturation: a complex pathway for a simple task? Biochem Soc Trans 30: 633-638
    • (2002) Biochem Soc Trans , vol.30 , pp. 633-638
    • Thony-Meyer, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.