메뉴 건너뛰기




Volumn 48, Issue 8, 2009, Pages 1820-1828

Probing the heme-binding site of the cytochrome c maturation protein CcmE

Author keywords

[No Author keywords available]

Indexed keywords

AXIAL LIGATIONS; BACTERIAL SPECIES; C-TYPE CYTOCHROMES; CYTOCHROME C; HEME BINDINGS; HEME CHAPERONES; HEME IRONS; HEME POCKETS; PLANT MITOCHONDRION; POINT MUTATIONS; PROTEIN FOLDS; REDUCTION POTENTIALS;

EID: 64349090263     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801609a     Document Type: Article
Times cited : (25)

References (51)
  • 1
    • 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. (2003) C-type cytochromes: Diverse structures and biogenesis systems pose evolutionary problems. Philos. Trans. R. Soc. London, Ser. B 358, 255-266.
    • (2003) Philos. Trans. R. Soc. London, Ser. B , vol.358 , pp. 255-266
    • Allen, J.W.1    Daltrop, O.2    Stevens, J.M.3    Ferguson, S.J.4
  • 2
    • 0031875674 scopus 로고    scopus 로고
    • Molecular mechanisms of cytochrome c biogenesis: Three distinct systems
    • Kranz, R., Lill, R., Goldman, B., Bonnard, G., and 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
  • 3
    • 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
  • 4
    • 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. (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.3    Ferguson, S.J.4
  • 5
    • 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. (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.1    Ginger, M.L.2    Ferguson, S.J.3
  • 6
    • 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. (2007) A specific c-type cytochrome maturation system is required for oxygenic photosynthesis. Proc. Natl. Acad. Sci. U.S.A. 104, 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
  • 7
    • 23844544711 scopus 로고    scopus 로고
    • Covalent cofactor attachment to proteins: Cytochrome c biogenesis
    • Stevens, J. M., Uchida, T., Daltrop, O., and Ferguson, S. J. (2005) Covalent cofactor attachment to proteins: Cytochrome c biogenesis. Biochem. Soc. Trans. 33, 792-795.
    • (2005) Biochem. Soc. Trans , vol.33 , pp. 792-795
    • Stevens, J.M.1    Uchida, T.2    Daltrop, O.3    Ferguson, S.J.4
  • 8
    • 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, R. A., Pellicioli, E. C., Hennecke, H., and 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. U.S.A. 96, 6462-6467.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 6462-6467
    • Schulz, H.1    Fabianek, R.A.2    Pellicioli, E.C.3    Hennecke, H.4    Thony-Meyer, L.5
  • 9
    • 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. (2007) Loss of ATP hydrolysis activity by CcmAB results in loss of c-type cytochrome synthesis and incomplete processing of CcmE. FEBS J. 274, 2322-2332.
    • (2007) FEBS J , vol.274 , pp. 2322-2332
    • Christensen, O.1    Harvat, E.M.2    Thony-Meyer, L.3    Ferguson, S.J.4    Stevens, J.M.5
  • 10
    • 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. (2006) 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
    • 0031554890 scopus 로고    scopus 로고
    • A thioreduction pathway tethered to the membrane for periplasmic cytochromes c biogenesis: In vitro and in vivo studies
    • Monika, E. M., Goldman, B. S., Beckman, D. L., and Kranz, R. G (1997) A thioreduction pathway tethered to the membrane for periplasmic cytochromes c biogenesis: In vitro and in vivo studies. J. Mol. Biol. 271, 679-692.
    • (1997) J. Mol. Biol , vol.271 , pp. 679-692
    • Monika, E.M.1    Goldman, B.S.2    Beckman, D.L.3    Kranz, R.G.4
  • 12
    • 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., and 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
  • 13
  • 14
    • 0037167010 scopus 로고    scopus 로고
    • Novel histidine-heme covalent linkage in a hemoglobin
    • Vu, B. C., Jones, A. D., and Lecomte, J. T. (2002) Novel histidine-heme covalent linkage in a hemoglobin. J. Am. Chem. Soc. 124, 8544-8545.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 8544-8545
    • Vu, B.C.1    Jones, A.D.2    Lecomte, J.T.3
  • 16
    • 0036849827 scopus 로고    scopus 로고
    • NMR structure of the heme chaperone CcmE reveals a novel functional motif
    • Enggist, E., Thony-Meyer, L., Guntert, P., and Pervushin, K (2002) NMR structure of the heme chaperone CcmE reveals a novel functional motif. Structure 10, 1551-1557.
    • (2002) Structure , vol.10 , pp. 1551-1557
    • Enggist, E.1    Thony-Meyer, L.2    Guntert, P.3    Pervushin, K.4
  • 17
    • 0032583439 scopus 로고    scopus 로고
    • Effects of ligation and folding on reduction potentials of heme proteins
    • Tezcan, F. A., Winkler, J. R., and Gray, H. B. (1998) Effects of ligation and folding on reduction potentials of heme proteins. J. Am. Chem. Soc. 120, 13383-13388.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 13383-13388
    • Tezcan, F.A.1    Winkler, J.R.2    Gray, H.B.3
  • 18
    • 0037046976 scopus 로고    scopus 로고
    • Tuning the reduction potential of engineered cytochrome c553
    • Fantuzzi, A., Sadeghi, S., Valetti, F., Rossi, G. L., and Gilardi, G (2002) Tuning the reduction potential of engineered cytochrome c553. Biochemistry 41, 8718-8724.
    • (2002) Biochemistry , vol.41 , pp. 8718-8724
    • Fantuzzi, A.1    Sadeghi, S.2    Valetti, F.3    Rossi, G.L.4    Gilardi, G.5
  • 19
    • 0023044641 scopus 로고
    • Control of the redox potential of cytochrome c and microscopic dielectric effects in proteins
    • Churg, A. K, and Warshel, A. (1986) Control of the redox potential of cytochrome c and microscopic dielectric effects in proteins. Biochemistry 25, 1675-1681.
    • (1986) Biochemistry , vol.25 , pp. 1675-1681
    • Churg, A.K.1    Warshel, A.2
  • 20
    • 0015385789 scopus 로고
    • Effects of nonpolar environments on the redox potentials of heme complexes
    • Kassner, R. J. (1972) Effects of nonpolar environments on the redox potentials of heme complexes. Proc. Natl. Acad. Sci. U.S.A. 69, 2263-2267.
    • (1972) Proc. Natl. Acad. Sci. U.S.A , vol.69 , pp. 2263-2267
    • Kassner, R.J.1
  • 21
    • 0018129356 scopus 로고
    • Haem exposure as the determinate of oxidation-reduction potential of haem proteins
    • Stellwagen, E. (1978) Haem exposure as the determinate of oxidation-reduction potential of haem proteins. Nature 275, 73-74.
    • (1978) Nature , vol.275 , pp. 73-74
    • Stellwagen, E.1
  • 22
    • 0037214399 scopus 로고    scopus 로고
    • Biochemical and mutational characterization of the heme chaperone CcmE reveals a heme binding site
    • Enggist, E., Schneider, M. J., Schulz, H., and Thony-Meyer, L. (2003) Biochemical and mutational characterization of the heme chaperone 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
  • 24
    • 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., and 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
  • 25
    • 0032578852 scopus 로고    scopus 로고
    • Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb3 oxidase in Escherichia coli
    • Arslan, E., Schulz, H., Zufferey, R., Kunzler, P., and Thony-Meyer, L. (1998) Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb3 oxidase in Escherichia coli. Biochem. Biophys. Res. Commun. 251, 744-747.
    • (1998) Biochem. Biophys. Res. Commun , vol.251 , pp. 744-747
    • Arslan, E.1    Schulz, H.2    Zufferey, R.3    Kunzler, P.4    Thony-Meyer, L.5
  • 26
    • 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. (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
  • 27
    • 27744576819 scopus 로고    scopus 로고
    • Functional characterization of the C-terminal domain of the cytochrome c maturation protein CcmE
    • Harvat, E. M., Stevens, J. M., Redfield, C., and Ferguson, S. J. (2005) Functional characterization of the C-terminal domain of the cytochrome c maturation protein CcmE. J. Biol. Chem. 280, 36747-36753.
    • (2005) J. Biol. Chem , vol.280 , pp. 36747-36753
    • Harvat, E.M.1    Stevens, J.M.2    Redfield, C.3    Ferguson, S.J.4
  • 28
    • 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. (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
  • 29
    • 0032555539 scopus 로고    scopus 로고
    • Prototype of a heme chaperone essential for cytochrome c maturation
    • Schulz, H., Hennecke, H., and 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
  • 30
    • 46149130370 scopus 로고
    • Haem staining in gels, a useful tool in the study of bacterial c-type cytochromes
    • Goodhew, C. F., Brown, K. R., and 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
  • 31
    • 0018115502 scopus 로고
    • Redox potentiometry: Determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems
    • Dutton, P. L. (1978) Redox potentiometry: Determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems. Methods Enzymol. 54, 411-435.
    • (1978) Methods Enzymol , vol.54 , pp. 411-435
    • Dutton, P.L.1
  • 32
    • 0001267512 scopus 로고
    • The oxidation potential of the system potassium ferrocyanide-potassium ferricyanide at various ionic strengths
    • Kolthoff, I. M., and Tomscicek, W. J. (1935) The oxidation potential of the system potassium ferrocyanide-potassium ferricyanide at various ionic strengths. J. Phys. Chem. 39, 945-954.
    • (1935) J. Phys. Chem , vol.39 , pp. 945-954
    • Kolthoff, I.M.1    Tomscicek, W.J.2
  • 33
  • 34
    • 0034610349 scopus 로고    scopus 로고
    • Heme redox potential control in de novo designed four-a helix bundle proteins
    • Shifman, J. M., Gibney, B. R., Sharp, R. E., and Dutton, P. L. (2000) Heme redox potential control in de novo designed four-a helix bundle proteins. Biochemistry 39, 14813-14821.
    • (2000) Biochemistry , vol.39 , pp. 14813-14821
    • Shifman, J.M.1    Gibney, B.R.2    Sharp, R.E.3    Dutton, P.L.4
  • 35
    • 1542274547 scopus 로고    scopus 로고
    • Heme protein assemblies
    • Reedy, C. J., and Gibney, B. R. (2004) Heme protein assemblies. Chem. Rev. 104, 617-649.
    • (2004) Chem. Rev , vol.104 , pp. 617-649
    • Reedy, C.J.1    Gibney, B.R.2
  • 36
    • 0017406836 scopus 로고
    • Structural basis for the variation in redox potential of cytochromes
    • Moore, G. R., and Williams, R. J. (1977) Structural basis for the variation in redox potential of cytochromes. FEBS Lett. 79, 229-232.
    • (1977) FEBS Lett , vol.79 , pp. 229-232
    • Moore, G.R.1    Williams, R.J.2
  • 38
    • 0030946074 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular heme-binding protein, HasA, involved in heme iron acquisition
    • Izadi, N., Henry, Y., Haladjian, J., Goldberg, M. E., Wandersman, C., Delepierre, M., and Lecroisey, A. (1997) Purification and characterization of an extracellular heme-binding protein, HasA, involved in heme iron acquisition. Biochemistry 36, 7050-7057.
    • (1997) Biochemistry , vol.36 , pp. 7050-7057
    • Izadi, N.1    Henry, Y.2    Haladjian, J.3    Goldberg, M.E.4    Wandersman, C.5    Delepierre, M.6    Lecroisey, A.7
  • 39
    • 33845892486 scopus 로고    scopus 로고
    • The crystal structure of the secreted dimeric form of the hemophore HasA reveals a domain swapping with an exchanged heme ligand
    • Czjzek, M., Letoffe, S., Wandersman, C., Delepierre, M., Lecroisey, A., and Izadi-Pruneyre, N. (2007) The crystal structure of the secreted dimeric form of the hemophore HasA reveals a domain swapping with an exchanged heme ligand. J. Mol. Biol. 365, 1176-1186.
    • (2007) J. Mol. Biol , vol.365 , pp. 1176-1186
    • Czjzek, M.1    Letoffe, S.2    Wandersman, C.3    Delepierre, M.4    Lecroisey, A.5    Izadi-Pruneyre, N.6
  • 40
    • 33646585766 scopus 로고    scopus 로고
    • Dynamic ligation properties of the Escherichia coli heme chaperone CcmE to non-covalently bound heme
    • Stevens, J. M., Uchida, T., Daltrop, O., Kitagawa, T., and Ferguson, S. J. (2006) Dynamic ligation properties of the Escherichia coli heme chaperone CcmE to non-covalently bound heme. J. Biol. Chem. 281, 6144-6151.
    • (2006) J. Biol. Chem , vol.281 , pp. 6144-6151
    • Stevens, J.M.1    Uchida, T.2    Daltrop, O.3    Kitagawa, T.4    Ferguson, S.J.5
  • 41
    • 0034693154 scopus 로고    scopus 로고
    • Loss of either of the two heme-binding cysteines from a class I c-type cytochrome has a surprisingly small effect on physicochemical properties
    • Tomlinson, E. J., and Ferguson, S. J. (2000) Loss of either of the two heme-binding cysteines from a class I c-type cytochrome has a surprisingly small effect on physicochemical properties. J. Biol. Chem. 275, 32530-32534.
    • (2000) J. Biol. Chem , vol.275 , pp. 32530-32534
    • Tomlinson, E.J.1    Ferguson, S.J.2
  • 42
    • 0024555936 scopus 로고
    • Characteristics in tyrosine coordinations of four hemoglobins M probed by resonance Raman spectroscopy
    • Nagai, M., Yoneyama, Y., and Kitagawa, T. (1989) Characteristics in tyrosine coordinations of four hemoglobins M probed by resonance Raman spectroscopy. Biochemistry 28, 2418-2422.
    • (1989) Biochemistry , vol.28 , pp. 2418-2422
    • Nagai, M.1    Yoneyama, Y.2    Kitagawa, T.3
  • 44
    • 0026038434 scopus 로고
    • Alteration of human myoglobin proximal histidine to cysteine or tyrosine by site-directed mutagenesis: Characterization and their catalytic activities
    • Adachi, S., Nagano, S., Watanabe, Y., Ishimori, K., and Morishima, I. (1991) Alteration of human myoglobin proximal histidine to cysteine or tyrosine by site-directed mutagenesis: Characterization and their catalytic activities. Biochem. Biophys. Res. Commun. 180, 138-144.
    • (1991) Biochem. Biophys. Res. Commun , vol.180 , pp. 138-144
    • Adachi, S.1    Nagano, S.2    Watanabe, Y.3    Ishimori, K.4    Morishima, I.5
  • 46
    • 0030714610 scopus 로고    scopus 로고
    • Alanine insertion scanning mutagenesis of lactose permease transmembrane helices
    • Braun, P., Persson, B., Kaback, H. R., and von Heijne, G (1997) Alanine insertion scanning mutagenesis of lactose permease transmembrane helices. J. Biol. Chem. 272, 29566-29571.
    • (1997) J. Biol. Chem , vol.272 , pp. 29566-29571
    • Braun, P.1    Persson, B.2    Kaback, H.R.3    von Heijne, G.4
  • 47
    • 0346843111 scopus 로고    scopus 로고
    • Induction of substrate specificity shifts by placement of alanine insertions within the consensus amphipathic region of the Escherichia coli GABA (γ-aminobutyric acid) transporter encoded by gabP
    • King, S. C., Hu, L. A., and Pugh, A. (2003) Induction of substrate specificity shifts by placement of alanine insertions within the consensus amphipathic region of the Escherichia coli GABA (γ-aminobutyric acid) transporter encoded by gabP. Biochem. J. 376, 645-653.
    • (2003) Biochem. J , vol.376 , pp. 645-653
    • King, S.C.1    Hu, L.A.2    Pugh, A.3
  • 48
    • 0029893893 scopus 로고    scopus 로고
    • Ala-insertion scanning mutagenesis of the glycophorin A transmembrane helix: A rapid way to map helix-helix interactions in integral membrane proteins
    • Mingarro, I., Whitley, P., Lemmon, M. A., and von Heijne, G (1996) Ala-insertion scanning mutagenesis of the glycophorin A transmembrane helix: A rapid way to map helix-helix interactions in integral membrane proteins. Protein Sci. 5, 1339-1341.
    • (1996) Protein Sci , vol.5 , pp. 1339-1341
    • Mingarro, I.1    Whitley, P.2    Lemmon, M.A.3    von Heijne, G.4
  • 49
    • 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. (2006) A variant System I for cytochrome c biogenesis in archaea and some bacteria has a novel CcmE and no CcmH. FEBS Lett. 580, 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
  • 50
    • 0038039207 scopus 로고    scopus 로고
    • The C-terminal flexible domain of the heme chaperone CcmE is important but not essential for its function
    • Enggist, E., and Thony-Meyer, L. (2003) The C-terminal flexible domain of the heme chaperone CcmE is important but not essential for its function. J. Bacteriol. 185, 3821-3827.
    • (2003) J. Bacteriol , vol.185 , pp. 3821-3827
    • Enggist, E.1    Thony-Meyer, L.2
  • 51
    • 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. (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. U.S.A. 99, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.