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Volumn 327, Issue 3, 2005, Pages 668-674

Successful recombinant production of Allochromatium vinosum cytochrome c′ requires coexpression of cmm genes in heme-rich Escherichia coli JCB712

Author keywords

Allochromatium vinosum; Cytochrome c ; Heme incorporation; Heme based sensor protein; Periplasmic protein expression

Indexed keywords

CYTOCHROME C'; HEME; ISOENZYME; LIGAND; MALTOSE BINDING PROTEIN; RECOMBINANT ENZYME; RECOMBINANT PROTEIN;

EID: 11844276066     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.12.062     Document Type: Article
Times cited : (10)

References (36)
  • 1
    • 0020453669 scopus 로고
    • New perspectives on c-type cytochromes
    • T.E. Meyer, and M.D. Kamen New perspectives on c-type cytochromes Adv. Protein Chem. 35 1982 105 212
    • (1982) Adv. Protein Chem. , vol.35 , pp. 105-212
    • Meyer, T.E.1    Kamen, M.D.2
  • 2
    • 0025903765 scopus 로고
    • Ligand binding properties of cytochromes c′
    • R.J. Kassner Ligand binding properties of cytochromes c′ Biochim. Biophys. Acta 1058 1991 8 12
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 8-12
    • Kassner, R.J.1
  • 3
    • 0022551670 scopus 로고
    • Kinetics of electron transfer between cytochromes c′ and the semiquinones of free flavin and clostridial flavodoxin
    • T.E. Meyer, G. Cheddar, R.G. Bartsch, E.D. Getzoff, M.A. Cusanovich, and G. Tollin Kinetics of electron transfer between cytochromes c′ and the semiquinones of free flavin and clostridial flavodoxin Biochemistry 25 1986 1383 1390
    • (1986) Biochemistry , vol.25 , pp. 1383-1390
    • Meyer, T.E.1    Cheddar, G.2    Bartsch, R.G.3    Getzoff, E.D.4    Cusanovich, M.A.5    Tollin, G.6
  • 4
    • 0036785322 scopus 로고    scopus 로고
    • Mechanism and biological role of nitric oxide binding to cytochrome c′
    • A.L. Mayburd, and R.J. Kassner Mechanism and biological role of nitric oxide binding to cytochrome c′ Biochemistry 41 2002 11582 11591
    • (2002) Biochemistry , vol.41 , pp. 11582-11591
    • Mayburd, A.L.1    Kassner, R.J.2
  • 5
    • 0033965782 scopus 로고    scopus 로고
    • Cytochrome c′ from Rhodobacter capsulatus confers increased resistance to nitric oxide
    • R. Cross, J. Aish, S.J. Paston, R.K. Poole, and J.W. Moir Cytochrome c′ from Rhodobacter capsulatus confers increased resistance to nitric oxide J. Bacteriol. 182 2000 1442 1447
    • (2000) J. Bacteriol. , vol.182 , pp. 1442-1447
    • Cross, R.1    Aish, J.2    Paston, S.J.3    Poole, R.K.4    Moir, J.W.5
  • 6
    • 0022517026 scopus 로고
    • Ligand-controlled dissociation of Chromatium vinosum cytochrome c′
    • M.L. Doyle, S.J. Gill, and M.A. Cusanovich Ligand-controlled dissociation of Chromatium vinosum cytochrome c′ Biochemistry 25 1986 2509 2516
    • (1986) Biochemistry , vol.25 , pp. 2509-2516
    • Doyle, M.L.1    Gill, S.J.2    Cusanovich, M.A.3
  • 7
    • 0026019555 scopus 로고
    • Cyanide-linked dimer-monomer equilibrium of Chromatium vinosum ferric cytochrome c′
    • M. Motie, R.J. Kassner, T.E. Meyer, and M.A. Cusanovich Cyanide-linked dimer-monomer equilibrium of Chromatium vinosum ferric cytochrome c′ Biochim. Biophys. Acta 1076 1991 97 102
    • (1991) Biochim. Biophys. Acta , vol.1076 , pp. 97-102
    • Motie, M.1    Kassner, R.J.2    Meyer, T.E.3    Cusanovich, M.A.4
  • 8
    • 0027380310 scopus 로고
    • Atomic structure of a cytochrome c′ with an unusual ligand-controlled dimer dissociation at 1.8 Å resolution
    • Z. Ren, T. Meyer, and D.E. McRee Atomic structure of a cytochrome c′ with an unusual ligand-controlled dimer dissociation at 1.8 Å resolution J. Mol. Biol. 234 1993 433 445
    • (1993) J. Mol. Biol. , vol.234 , pp. 433-445
    • Ren, Z.1    Meyer, T.2    McRee, D.E.3
  • 9
    • 7044233148 scopus 로고    scopus 로고
    • Structural insights into the regulation and the activation mechanism of mammalian guanylyl cyclases
    • P.S. Padayatti, P. Pattanaik, X. Ma, and F. van den Akker Structural insights into the regulation and the activation mechanism of mammalian guanylyl cyclases Pharmacol. Ther. 104 2004 83 99
    • (2004) Pharmacol. Ther. , vol.104 , pp. 83-99
    • Padayatti, P.S.1    Pattanaik, P.2    Ma, X.3    Van Den Akker, F.4
  • 10
    • 4344573215 scopus 로고    scopus 로고
    • Activation mechanisms of transcriptional regulator CooA revealed by small-angle X-ray scattering
    • S. Akiyama, T. Fujisawa, K. Ishimori, I. Morishima, and S. Aono Activation mechanisms of transcriptional regulator CooA revealed by small-angle X-ray scattering J. Mol. Biol. 341 2004 651 668
    • (2004) J. Mol. Biol. , vol.341 , pp. 651-668
    • Akiyama, S.1    Fujisawa, T.2    Ishimori, K.3    Morishima, I.4    Aono, S.5
  • 11
    • 0942298565 scopus 로고    scopus 로고
    • Signal transduction by heme-containing PAS-domain proteins
    • M.-A. Gilles-Gonzalez, and G. Gonzalez Signal transduction by heme-containing PAS-domain proteins J. Appl. Physiol. 96 2004 774 783
    • (2004) J. Appl. Physiol. , vol.96 , pp. 774-783
    • Gilles-Gonzalez, M.-A.1    Gonzalez, G.2
  • 12
    • 0037260847 scopus 로고    scopus 로고
    • Mechanisms of ligand discrimination by heme proteins
    • R. Jain, and M.K. Chan Mechanisms of ligand discrimination by heme proteins J. Biol. Inorg. Chem. 8 2003 1 11
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 1-11
    • Jain, R.1    Chan, M.K.2
  • 13
    • 0036667736 scopus 로고    scopus 로고
    • Engineering and design of ligand-induced conformational change in proteins
    • L.S. Mizoue, and W.J. Chazin Engineering and design of ligand-induced conformational change in proteins Curr. Opin. Struct. Biol. 12 2002 459 463
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 459-463
    • Mizoue, L.S.1    Chazin, W.J.2
  • 14
    • 0029940242 scopus 로고    scopus 로고
    • High-resolution crystal structures of two polymorphs of cytochrome c′ from the purple phototrophic bacterium Rhodobacter capsulatus
    • T.H. Tahirov, S. Misaki, T.E. Meyer, M.A. Cusanovich, Y. Higuchi, and N. Yasuoka High-resolution crystal structures of two polymorphs of cytochrome c′ from the purple phototrophic bacterium Rhodobacter capsulatus J. Mol. Biol. 259 1996 467 479
    • (1996) J. Mol. Biol. , vol.259 , pp. 467-479
    • Tahirov, T.H.1    Misaki, S.2    Meyer, T.E.3    Cusanovich, M.A.4    Higuchi, Y.5    Yasuoka, N.6
  • 16
    • 0022419653 scopus 로고
    • Structure of ferricytochrome c′ from Rhodospirillum molischianum at 1.67 Å resolution
    • B.C. Finzel, P.C. Weber, K.D. Hardman, and F.R. Salemme Structure of ferricytochrome c′ from Rhodospirillum molischianum at 1.67 Å resolution J. Mol. Biol. 186 1985 627 643
    • (1985) J. Mol. Biol. , vol.186 , pp. 627-643
    • Finzel, B.C.1    Weber, P.C.2    Hardman, K.D.3    Salemme, F.R.4
  • 18
    • 0030046275 scopus 로고    scopus 로고
    • Three-dimensional structure of cytochrome c′ from two Alcaligenes species and the implications for four-helix bundle structures
    • A.J. Dobbs, B.F. Anderson, H.R. Faber, and E.N. Baker Three-dimensional structure of cytochrome c′ from two Alcaligenes species and the implications for four-helix bundle structures Acta Crystallogr. Sect. D: Biol. Crystallogr. 52 1996 356 368
    • (1996) Acta Crystallogr. Sect. D: Biol. Crystallogr. , vol.52 , pp. 356-368
    • Dobbs, A.J.1    Anderson, B.F.2    Faber, H.R.3    Baker, E.N.4
  • 19
    • 0030830925 scopus 로고    scopus 로고
    • Crystal structure of cytochrome c′ from Rhodocyclus gelatinosus and comparison with other cytochromes c′
    • M. Archer, L. Banci, E. Dikaya, and M.J. Romao Crystal structure of cytochrome c′ from Rhodocyclus gelatinosus and comparison with other cytochromes c′ J. Biol. Inorg. Chem. 2 1997 611 622
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 611-622
    • Archer, M.1    Banci, L.2    Dikaya, E.3    Romao, M.J.4
  • 20
    • 0026598140 scopus 로고
    • Three-dimensional structure of ferricytochrome c′ from Rhodospirillum rubrum at 2.8 Å resolution
    • M. Yasui, S. Harada, Y. Kai, N. Kasai, M. Kusunoki, and Y. Matsuura Three-dimensional structure of ferricytochrome c′ from Rhodospirillum rubrum at 2.8 Å resolution J. Biochem. (Tokyo, Jpn.) 111 1992 317 324
    • (1992) J. Biochem. (Tokyo, Jpn.) , vol.111 , pp. 317-324
    • Yasui, M.1    Harada, S.2    Kai, Y.3    Kasai, N.4    Kusunoki, M.5    Matsuura, Y.6
  • 21
    • 0037069387 scopus 로고    scopus 로고
    • Structural features of cytochrome c′ folding intermediates revealed by fluorescence energy-transfer kinetics
    • J.C. Lee, K.C. Engman, F.A. Tezcan, H.B. Gray, and J.R. Winkler Structural features of cytochrome c′ folding intermediates revealed by fluorescence energy-transfer kinetics Proc. Natl. Acad. Sci. USA 99 2002 14778 14782
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14778-14782
    • Lee, J.C.1    Engman, K.C.2    Tezcan, F.A.3    Gray, H.B.4    Winkler, J.R.5
  • 22
    • 0033135697 scopus 로고    scopus 로고
    • Ratiometric and fluorescence-lifetime-based biosensors incorporating cytochrome c′ and the detection of extra- and intracellular macrophage nitric oxide
    • S.L. Barker, H.A. Clark, S.F. Swallen, R. Kopelman, A.W. Tsang, and J.A. Swanson Ratiometric and fluorescence-lifetime-based biosensors incorporating cytochrome c′ and the detection of extra- and intracellular macrophage nitric oxide Anal. Chem. 71 1999 1767 1772
    • (1999) Anal. Chem. , vol.71 , pp. 1767-1772
    • Barker, S.L.1    Clark, H.A.2    Swallen, S.F.3    Kopelman, R.4    Tsang, A.W.5    Swanson, J.A.6
  • 24
    • 0034213533 scopus 로고    scopus 로고
    • Complex formation between Chromatium vinosum ferric cytochrome c′ and bromophenol blue
    • A.L. Mayburd, Y. Tan, and R.J. Kassner Complex formation between Chromatium vinosum ferric cytochrome c′ and bromophenol blue Arch. Biochem. Biophys. 378 2000 40 44
    • (2000) Arch. Biochem. Biophys. , vol.378 , pp. 40-44
    • Mayburd, A.L.1    Tan, Y.2    Kassner, R.J.3
  • 26
    • 0036671471 scopus 로고    scopus 로고
    • Cytochrome c maturation: A complex pathway for a simple task?
    • L. Thöny-Meyer Cytochrome c maturation: a complex pathway for a simple task? Biochem. Soc. Trans. 30 2002 633 638
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 633-638
    • Thöny-Meyer, L.1
  • 27
    • 0032578852 scopus 로고    scopus 로고
    • Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb3 oxidase in Escherichia coli
    • E. Arslan, H. Schulz, R. Zufferey, P. Kunzler, and L. Thöny-Meyer Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb3 oxidase in Escherichia coli Biochem. Biophys. Res. Commun. 251 1998 744 747
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 744-747
    • Arslan, E.1    Schulz, H.2    Zufferey, R.3    Kunzler, P.4    Thöny-Meyer, L.5
  • 29
    • 0030033752 scopus 로고    scopus 로고
    • Escherichia coli K-12 genes essential for the synthesis of c-type cytochromes and a third nitrate reductase located in the periplasm
    • J. Grove, S. Tanapongpipat, G. Thomas, L. Griffiths, H. Crooke, and J. Cole Escherichia coli K-12 genes essential for the synthesis of c-type cytochromes and a third nitrate reductase located in the periplasm Mol. Microbiol. 19 1996 467 481
    • (1996) Mol. Microbiol. , vol.19 , pp. 467-481
    • Grove, J.1    Tanapongpipat, S.2    Thomas, G.3    Griffiths, L.4    Crooke, H.5    Cole, J.6
  • 30
    • 0032054834 scopus 로고    scopus 로고
    • An Escherichia coli ccm (cytochrome c maturation) deletion strain substantially expresses Hydrogenobacter thermophilus cytochrome c552 in the cytoplasm: Availability of haem influences cytochrome c552 maturation
    • N. Sinha, and S.J. Ferguson An Escherichia coli ccm (cytochrome c maturation) deletion strain substantially expresses Hydrogenobacter thermophilus cytochrome c552 in the cytoplasm: availability of haem influences cytochrome c552 maturation FEMS Microbiol. Lett. 161 1998 1 6
    • (1998) FEMS Microbiol. Lett. , vol.161 , pp. 1-6
    • Sinha, N.1    Ferguson, S.J.2
  • 31
    • 84969021820 scopus 로고
    • Spectroscopic properties of purified cytochromes of photosynthetic bacteria
    • H. Gest A. San Pietro L.P. Vernon Antioch Press Yellow Springs, OH
    • R.G. Bartsch Spectroscopic properties of purified cytochromes of photosynthetic bacteria H. Gest A. San Pietro L.P. Vernon Bacterial Photosynthesis 1963 Antioch Press Yellow Springs, OH 475 494
    • (1963) Bacterial Photosynthesis , pp. 475-494
    • Bartsch, R.G.1
  • 32
    • 0022181814 scopus 로고
    • Binding of cyanide to cytochrome c′ from Chromatium vinosum
    • R.J. Kassner, M.G. Kykta, and M.A. Cusanovich Binding of cyanide to cytochrome c′ from Chromatium vinosum Biochim. Biophys. Acta 831 1985 155 158
    • (1985) Biochim. Biophys. Acta , vol.831 , pp. 155-158
    • Kassner, R.J.1    Kykta, M.G.2    Cusanovich, M.A.3
  • 33
    • 0029199530 scopus 로고
    • Escherichia coli electrotransformation
    • E.M. Miller, and J.A. Nickoloff Escherichia coli electrotransformation Methods Mol. Biol. 47 1995 105 113
    • (1995) Methods Mol. Biol. , vol.47 , pp. 105-113
    • Miller, E.M.1    Nickoloff, J.A.2
  • 34
    • 0033858359 scopus 로고    scopus 로고
    • Van't Hoff enthalpies without baselines
    • D.M. John, and K.M. Weeks Van't Hoff enthalpies without baselines Protein Sci. 9 2000 1416 1419
    • (2000) Protein Sci. , vol.9 , pp. 1416-1419
    • John, D.M.1    Weeks, K.M.2
  • 35
    • 0001023705 scopus 로고
    • Cytochromes
    • R.K. Clayton W.R. Sistrom Plenum press New York
    • R.G. Bartsch Cytochromes R.K. Clayton W.R. Sistrom The Photosynthetic Bacteria 1978 Plenum press New York 249 279
    • (1978) The Photosynthetic Bacteria , pp. 249-279
    • Bartsch, R.G.1
  • 36
    • 0010333120 scopus 로고
    • Isolation and properties of two soluble heme proteins in extracts of the photoanaerobe Chromatium
    • R.G. Bartsch, and M.D. Kamen Isolation and properties of two soluble heme proteins in extracts of the photoanaerobe Chromatium J. Biol. Chem. 235 1960 825 831
    • (1960) J. Biol. Chem. , vol.235 , pp. 825-831
    • Bartsch, R.G.1    Kamen, M.D.2


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