메뉴 건너뛰기




Volumn 73, Issue 1, 2010, Pages 78-82

Co-expression of ferrochelatase allows for complete heme incorporation into recombinant proteins produced in E. coli

Author keywords

Ferrochelatase; Free base porphyrin; Heme incorporation; Heme proteins

Indexed keywords

ESCHERICHIA COLI;

EID: 77955418491     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.03.010     Document Type: Article
Times cited : (42)

References (34)
  • 3
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: Structure, function and inhibition
    • W.K. Alderton, C.E. Cooper, R.G. Knowles, Nitric oxide synthases: structure, function and inhibition, Biochemical Journal 357 (2001) 593-615.
    • (2001) Biochemical Journal , vol.357 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 4
    • 0033229863 scopus 로고    scopus 로고
    • Fix L, a haemoglobin that acts as an oxygen sensor: Signalling mechanism and structural basis of its homology with PAS domains
    • M.F. Perutz, M. Paoli, A.M. Lesk, Fix L, a haemoglobin that acts as an oxygen sensor: signalling mechanism and structural basis of its homology with PAS domains, Chemistry & Biology 6 (1999) R291-R297.
    • (1999) Chemistry & Biology , vol.6
    • Perutz, M.F.1    Paoli, M.2    Lesk, A.M.3
  • 6
    • 0026052654 scopus 로고
    • Expression of rat heme oxygenase in Escherichia coli as a catalytically active, full-length form that binds to bacterial-membranes
    • K. Ishikawa, M. Sato, T. Yoshida, Expression of rat heme oxygenase in Escherichia coli as a catalytically active, full-length form that binds to bacterial-membranes, European Journal of Biochemistry 202 (1991) 161-165.
    • (1991) European Journal of Biochemistry , vol.202 , pp. 161-165
    • Ishikawa, K.1    Sato, M.2    Yoshida, T.3
  • 7
    • 0025275451 scopus 로고
    • Expression of a synthetic gene for horseradish peroxidase-C in Escherichia coli and folding and activation of the recombinant enzyme with Ca-2+ and heme
    • A.T. Smith, N. Santama, S. Dacey, M. Edwards, R.C. Bray, R.N.F. Thorneley, J.F. Burke, Expression of a synthetic gene for horseradish peroxidase-C in Escherichia coli and folding and activation of the recombinant enzyme with Ca-2+ and heme, Journal of Biological Chemistry 265 (1990) 13335-13343.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 13335-13343
    • Smith, A.T.1    Santama, N.2    Dacey, S.3    Edwards, M.4    Bray, R.C.5    Thorneley, R.N.F.6    Burke, J.F.7
  • 8
    • 0028984985 scopus 로고
    • Delta-aminolevulinate increases heme saturation and yield of human cystathionine beta-synthase expressed in Escherichia coli
    • V. Kery, D. Elleder, J.P. Kraus, Delta-aminolevulinate increases heme saturation and yield of human cystathionine beta-synthase expressed in Escherichia coli, Archives of Biochemistry and Biophysics 316 (1995) 24-29.
    • (1995) Archives of Biochemistry and Biophysics , vol.316 , pp. 24-29
    • Kery, V.1    Elleder, D.2    Kraus, J.P.3
  • 13
    • 2442443720 scopus 로고    scopus 로고
    • System for the expression of recombinant hemoproteins in Escherichia coli
    • C.L. Varnado, D.C. Goodwin, System for the expression of recombinant hemoproteins in Escherichia coli, Protein Expression and Purification 35 (2004) 76-83.
    • (2004) Protein Expression and Purification , vol.35 , pp. 76-83
    • Varnado, C.L.1    Goodwin, D.C.2
  • 14
    • 77955415057 scopus 로고    scopus 로고
    • Expression of recombinant hemoproteins in E. coli using a heme protein expression system
    • C. Varnado, J. Olson, D. Goodwin, Expression of recombinant hemoproteins in E. coli using a heme protein expression system, Biophysical Journal (2007) 384A.
    • (2007) Biophysical Journal , vol.384 A
    • Varnado, C.1    Olson, J.2    Goodwin, D.3
  • 15
    • 0030686417 scopus 로고    scopus 로고
    • Stabilization of apoglobin by low temperature increases yield of soluble recombinant hemoglobin in Escherichia coli
    • M.J. Weickert, M. Pagratis, S.R. Curry, R. Blackmore, Stabilization of apoglobin by low temperature increases yield of soluble recombinant hemoglobin in Escherichia coli, Applied and Environmental Microbiology 63 (1997) 4313-4320.
    • (1997) Applied and Environmental Microbiology , vol.63 , pp. 4313-4320
    • Weickert, M.J.1    Pagratis, M.2    Curry, S.R.3    Blackmore, R.4
  • 16
    • 0036098845 scopus 로고    scopus 로고
    • The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus highlights striking structural plasticity of the alpha-helical globin fold
    • A. Pesce, M. Nardini, S. Dewilde, E. Geuens, K. Yamauchi, P. Ascenzi, A.F. Riggs, L. Moens, M. Bolognesi, The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus highlights striking structural plasticity of the alpha-helical globin fold, Structure 10 (2002) 725-735.
    • (2002) Structure , vol.10 , pp. 725-735
    • Pesce, A.1    Nardini, M.2    Dewilde, S.3    Geuens, E.4    Yamauchi, K.5    Ascenzi, P.6    Riggs, A.F.7    Moens, L.8    Bolognesi, M.9
  • 17
    • 0028852912 scopus 로고
    • Bacterial expression of scapharca dimeric hemoglobin - A simple-model system for investigating protein cooperativity
    • C.M. Summerford, A. Pardanani, A.H. Betts, A.R. Poteete, G. Colotti, W.E. Royer, Bacterial expression of scapharca dimeric hemoglobin - a simple-model system for investigating protein cooperativity, Protein Engineering 8 (1995) 593-599.
    • (1995) Protein Engineering , vol.8 , pp. 593-599
    • Summerford, C.M.1    Pardanani, A.2    Betts, A.H.3    Poteete, A.R.4    Colotti, G.5    Royer, W.E.6
  • 18
    • 0031803820 scopus 로고    scopus 로고
    • High-fidelity translation of recombinant human hemoglobin in Escherichia coli
    • M.J. Weickert, I. Apostol, High-fidelity translation of recombinant human hemoglobin in Escherichia coli, Applied and Environmental Microbiology 64 (1998) 1589-1593.
    • (1998) Applied and Environmental Microbiology , vol.64 , pp. 1589-1593
    • Weickert, M.J.1    Apostol, I.2
  • 19
    • 0032976495 scopus 로고    scopus 로고
    • A mutation that improves soluble recombinant hemoglobin accumulation in Escherichia coli in heme excess
    • M.J. Weickert, M. Pagratis, C.B. Glascock, R. Blackmore, A mutation that improves soluble recombinant hemoglobin accumulation in Escherichia coli in heme excess, Applied and Environmental Microbiology 65 (1999) 640-647.
    • (1999) Applied and Environmental Microbiology , vol.65 , pp. 640-647
    • Weickert, M.J.1    Pagratis, M.2    Glascock, C.B.3    Blackmore, R.4
  • 20
    • 33845959112 scopus 로고    scopus 로고
    • An Escherichia coli expression-based method for heme substitution
    • J.J. Woodward, N.I. Martin, M.A. Marletta, An Escherichia coli expression-based method for heme substitution, Nature Methods 4 (2007) 43-45.
    • (2007) Nature Methods , vol.4 , pp. 43-45
    • Woodward, J.J.1    Martin, N.I.2    Marletta, M.A.3
  • 21
    • 33646904895 scopus 로고    scopus 로고
    • Structure and reactivity of a thermostable prokaryotic nitric-oxide synthase that forms a long-lived oxy-heme complex
    • J. Sudhamsu, B.R. Crane, Structure and reactivity of a thermostable prokaryotic nitric-oxide synthase that forms a long-lived oxy-heme complex, Journal of Biological Chemistry 281 (2006) 9623-9632.
    • (2006) Journal of Biological Chemistry , vol.281 , pp. 9623-9632
    • Udhamsu, J.S.1    Crane, B.R.2
  • 22
    • 56749134247 scopus 로고    scopus 로고
    • Substrate-ligand interactions in Geobacillus stearthermophilus nitric oxide synthase
    • M. Kabir, J. Sudhamsu, B.R. Crane, S.R. Yeh, D.L. Rousseau, Substrate-ligand interactions in Geobacillus stearothermophilus nitric oxide synthase, Biochemistry 47 (2008) 12389-12397.
    • (2008) Biochemistry , vol.47 , pp. 12389-12397
    • Kabir, M.1    Sudhamsu, J.2    Crane, B.R.3    Yeh, S.R.4    Rousseau, D.L.5
  • 23
    • 70349921627 scopus 로고    scopus 로고
    • EPR and ENDOR characterization of the reactive intermediates in the generation of NO by cryoreduced oxy-nitric oxide synthase from G. stearothermophilus
    • R.H. Davydov, J. Sudhamsu, N.S. Lees, B.R. Crane, B.M. Hoffman, EPR and ENDOR characterization of the reactive intermediates in the generation of NO by cryoreduced oxy-nitric oxide synthase from G. stearothermophilus, Journal of the American Chemical Society 131 (2009) 14493-14507.
    • (2009) Journal of the American Chemical Society , vol.131 , pp. 14493-14507
    • Davydov, R.H.1    Sudhamsu, J.2    Lees, N.S.3    Crane, B.R.4    Hoffman, B.M.5
  • 24
    • 0037125928 scopus 로고    scopus 로고
    • Structure of a nitric oxide synthase heme protein from Bacillus subtilis
    • K. Pant, A.M. Bilwes, S. Adak, D.J. Stuehr, B.R. Crane, Structure of a nitric oxide synthase heme protein from Bacillus subtilis, Biochemistry 41 (2002) 11071-11079.
    • (2002) Biochemistry , vol.41 , pp. 11071-11079
    • Pant, K.1    Bilwes, A.M.2    Adak, S.3    Stuehr, D.J.4    Crane, B.R.5
  • 25
    • 9644264047 scopus 로고    scopus 로고
    • Regioselective nitration of tryptophan by a complex between bacterial nitric-oxide synthase and tryptophanyl-tRNA synthetase
    • M.R. Buddha, T. Tao, R.J. Parry, B.R. Crane, Regioselective nitration of tryptophan by a complex between bacterial nitric-oxide synthase and tryptophanyl-tRNA synthetase, Journal of Biological Chemistry 279 (2004) 49567-49570.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 49567-49570
    • Buddha, M.R.1    Tao, T.2    Parry, R.J.3    Crane, B.R.4
  • 26
    • 32244445822 scopus 로고    scopus 로고
    • Resonance Raman study of Bacillus subtilis NO synthase-like protein: Similarities and differences with mammalian NO synthases
    • M. Santolini, M. Roman, D.J. Stuehr, T.A. Mattioli, Resonance Raman study of Bacillus subtilis NO synthase-like protein: similarities and differences with mammalian NO synthases, Biochemistry 45 (2006) 1480-1489.
    • (2006) Biochemistry , vol.45 , pp. 1480-1489
    • Santolini, M.1    Roman, M.2    Stuehr, D.J.3    Mattioli, T.A.4
  • 28
    • 0345515979 scopus 로고    scopus 로고
    • Alternative modes of substrate distortion in enzyme and antibody catalyzed ferrochelation reactions
    • M.E. Blackwood, T.S. Rush, F. Romesberg, P.G. Schultz, T.G. Spiro, Alternative modes of substrate distortion in enzyme and antibody catalyzed ferrochelation reactions, Biochemistry 37 (1998) 779-782.
    • (1998) Biochemistry , vol.37 , pp. 779-782
    • Blackwood, M.E.1    Rush, T.S.2    Romesberg, F.3    Schultz, P.G.4    Spiro, T.G.5
  • 29
    • 0037008009 scopus 로고    scopus 로고
    • Binding of protoporphyrin IX and metal derivatives to the active site of wildtype mouse ferrochelatase at low porphyrin-to-protein ratios
    • Y. Lu, A. Sousa, R. Franco, A. Mangravita, G.C. Ferreira, I. Moura, J.A. Shelnutt, Binding of protoporphyrin IX and metal derivatives to the active site of wildtype mouse ferrochelatase at low porphyrin-to-protein ratios, Biochemistry 41 (2002) 8253-8262.
    • (2002) Biochemistry , vol.41 , pp. 8253-8262
    • Lu, Y.1    Sousa, A.2    Franco, R.3    Mangravita, A.4    Ferreira, G.C.5    Moura, I.6    Shelnutt, J.A.7
  • 31
    • 0025101925 scopus 로고
    • Heme production in animal-tissues - The regulation of biogenesis of delta-aminolevulinate synthase
    • I.Z. Ades, Heme production in animal-tissues - the regulation of biogenesis of delta-aminolevulinate synthase, International Journal of Biochemistry 22 (1990) 565-578.
    • (1990) International Journal of Biochemistry , vol.22 , pp. 565-578
    • Ades, I.Z.1
  • 33
    • 0035289298 scopus 로고    scopus 로고
    • Is delta-aminolevulinic acid dehydratase rate limiting in heme biosynthesis following exposure of cells to delta-aminolevulinic acid?
    • S.L. Gibson, J.J. Havens, L. Metz, R. Hilf, Is delta-aminolevulinic acid dehydratase rate limiting in heme biosynthesis following exposure of cells to delta-aminolevulinic acid?, Photochemistry and Photobiology 73 (2001) 312-317.
    • (2001) Photochemistry and Photobiology , vol.73 , pp. 312-317
    • Gibson, S.L.1    Havens, J.J.2    Metz, L.3    Hilf, R.4
  • 34
    • 44549088704 scopus 로고    scopus 로고
    • The biochemistry of heme biosynthesis
    • S.L. Gibson, J.J. Havens, L. Metz, R. Hilf, Is delta-aminolevulinic acid dehydratase rate limiting in heme biosynthesis following exposure of cells to delta-aminolevulinic acid?, Photochemistry and Photobiology 73 (2001) 312-317 [34] I.U. Heinemann, M. Jahn, D. Jahn, The biochemistry of heme biosynthesis, Archives of Biochemistry and Biophysics 474 (2008) 238-251.
    • (2008) Archives of Biochemistry and Biophysics , vol.474 , pp. 238-251
    • Heinemann, I.U.1    Jahn, M.2    Jahn, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.