메뉴 건너뛰기




Volumn 1674, Issue 3, 2004, Pages 319-326

The α-helical membrane spanning domain of cytochrome b 5 interacts with cytochrome P450 via nonspecific interactions

Author keywords

Cytochrome b 5; Cytochrome P450 2B4; Membrane protein; Mutagenesis; Protein protein interaction

Indexed keywords

ALANINE; AMINO ACID DERIVATIVE; ANESTHETIC AGENT; CYTOCHROME B5; CYTOCHROME P450; METHOXYFLURANE;

EID: 7944239530     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2004.08.001     Document Type: Article
Times cited : (14)

References (37)
  • 2
    • 0033970047 scopus 로고    scopus 로고
    • Mammalian microsomal cytochrome P450 monooxygenase: Structural adaptations for membrane binding and functional diversity
    • P.A. Williams, J. Cosme, V. Sridhar, E.F. Johnson, and D.E. McRee Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity Mol. Cell 5 2000 121 131
    • (2000) Mol. Cell , vol.5 , pp. 121-131
    • Williams, P.A.1    Cosme, J.2    Sridhar, V.3    Johnson, E.F.4    McRee, D.E.5
  • 3
    • 0028947399 scopus 로고
    • Subcellular localization, aggregation state, and catalytic activity of microsomal P450 cytochromes modified in the NH2-terminal region and expressed in Escherichia coli
    • S.J. Pernecky, N.M. Olken, L.L. Bestervelt, and M.J. Coon Subcellular localization, aggregation state, and catalytic activity of microsomal P450 cytochromes modified in the NH2-terminal region and expressed in Escherichia coli Arch. Biochem. Biophys. 318 1995 446 456
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 446-456
    • Pernecky, S.J.1    Olken, N.M.2    Bestervelt, L.L.3    Coon, M.J.4
  • 5
    • 0028970539 scopus 로고
    • 5, its functions, structure and membrane topology
    • 5, its functions, structure and membrane topology Biochimie 77 1995 604 620
    • (1995) Biochimie , vol.77 , pp. 604-620
    • Vergeres, G.1    Waskell, L.2
  • 11
    • 0141988883 scopus 로고    scopus 로고
    • Determination of the rate of reduction of oxyferrous cytochrome P450 2B4 by 5-deazariboflavin adenine dinucleotide T491V cytochrome P450 reductase
    • H. Zhang, L. Gruenke, D. Arscott, A. Shen, C. Kasper, D.L. Harris, M. Glavanovich, R. Johnson, and L. Waskell Determination of the rate of reduction of oxyferrous cytochrome P450 2B4 by 5-deazariboflavin adenine dinucleotide T491V cytochrome P450 reductase Biochemistry 42 2003 11594 11603
    • (2003) Biochemistry , vol.42 , pp. 11594-11603
    • Zhang, H.1    Gruenke, L.2    Arscott, D.3    Shen, A.4    Kasper, C.5    Harris, D.L.6    Glavanovich, M.7    Johnson, R.8    Waskell, L.9
  • 12
    • 0028063482 scopus 로고
    • Structural organization of the pentameric transmembrane alpha-helices of phospholamban, a cardiac ion channel
    • I.T. Arkin, P.D. Adams, K.R. MacKenzie, M.A. Lemmon, A.T. Brunger, and D.M. Engelman Structural organization of the pentameric transmembrane alpha-helices of phospholamban, a cardiac ion channel EMBO J. 13 1994 4757 4764
    • (1994) EMBO J. , vol.13 , pp. 4757-4764
    • Arkin, I.T.1    Adams, P.D.2    MacKenzie, K.R.3    Lemmon, M.A.4    Brunger, A.T.5    Engelman, D.M.6
  • 13
    • 0016657917 scopus 로고
    • Solubilization of membranes by detergents
    • A. Helenius, and K. Simons Solubilization of membranes by detergents Biochim. Biophys. Acta 415 1975 29 79
    • (1975) Biochim. Biophys. Acta , vol.415 , pp. 29-79
    • Helenius, A.1    Simons, K.2
  • 15
    • 0026612528 scopus 로고
    • 5 in yeast and characterization of mutants of the membrane-anchoring domain
    • 5 in yeast and characterization of mutants of the membrane-anchoring domain J. Biol. Chem. 267 1992 12583 12591
    • (1992) J. Biol. Chem. , vol.267 , pp. 12583-12591
    • Vergeres, G.1    Waskell, L.2
  • 16
    • 0017273203 scopus 로고
    • 5 in aqueous solution. Gel filtration and ultracentrifugational studies
    • 5 in aqueous solution. Gel filtration and ultracentrifugational studies J. Biol. Chem. 251 1976 2113 2118
    • (1976) J. Biol. Chem. , vol.251 , pp. 2113-2118
    • Calabro, M.A.1    Katz, J.T.2    Holloway, P.W.3
  • 17
    • 0019321102 scopus 로고
    • Interactions of cytochrome P-450, NADPH-cytochrome P-450 reductase, phospholipid, and substrate in the reconstituted liver microsomal enzyme system
    • J.S. French, F.P. Guengerich, and M.J. Coon Interactions of cytochrome P-450, NADPH-cytochrome P-450 reductase, phospholipid, and substrate in the reconstituted liver microsomal enzyme system J. Biol. Chem. 255 1980 4112 4119
    • (1980) J. Biol. Chem. , vol.255 , pp. 4112-4119
    • French, J.S.1    Guengerich, F.P.2    Coon, M.J.3
  • 19
    • 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
    • I. Mingarro, P. Whitley, M.A. Lemmon, and G. von Heijne 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 1996 1339 1341
    • (1996) Protein Sci. , vol.5 , pp. 1339-1341
    • Mingarro, I.1    Whitley, P.2    Lemmon, M.A.3    Von Heijne, G.4
  • 21
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • B. Miroux, and J.E. Walker Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels J. Mol. Biol. 260 1996 289 298
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 22
    • 0034043337 scopus 로고    scopus 로고
    • High-level expression in Escherichia coli and purification of the membrane-bound form of cytochrome b(5)
    • S.B. Mulrooney, and L. Waskell High-level expression in Escherichia coli and purification of the membrane-bound form of cytochrome b(5) Protein Expr. Purif. 19 2000 173 178
    • (2000) Protein Expr. Purif. , vol.19 , pp. 173-178
    • Mulrooney, S.B.1    Waskell, L.2
  • 23
    • 0017869007 scopus 로고
    • The measurement of difference spectra: Application to the cytochromes of microsomes
    • R.W. Estabrook, and J. Werringloer The measurement of difference spectra: application to the cytochromes of microsomes Methods Enzymol. 52 1978 212 220
    • (1978) Methods Enzymol. , vol.52 , pp. 212-220
    • Estabrook, R.W.1    Werringloer, J.2
  • 24
    • 0030714610 scopus 로고    scopus 로고
    • Alanine insertion scanning mutagenesis of lactose permease transmembrane helices
    • P. Braun, B. Persson, H.R. Kaback, and G. von Heijne Alanine insertion scanning mutagenesis of lactose permease transmembrane helices J. Biol. Chem. 272 1997 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
  • 33
    • 0034667871 scopus 로고    scopus 로고
    • How to measure and analyze tryptophan fluorescence in membranes properly, and why bother?
    • A.S. Ladokhin, S. Jayasinghe, and S.H. White How to measure and analyze tryptophan fluorescence in membranes properly, and why bother? Anal. Biochem. 285 2000 235 245
    • (2000) Anal. Biochem. , vol.285 , pp. 235-245
    • Ladokhin, A.S.1    Jayasinghe, S.2    White, S.H.3
  • 34
    • 0035979146 scopus 로고    scopus 로고
    • The CαH...O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions
    • A. Senes, I. Ubarretxena-Belandia, and D.M. Engelman The CαH...O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions Proc. Natl. Acad. Sci. U. S. A. 98 2001 9056 9061
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9056-9061
    • Senes, A.1    Ubarretxena-Belandia, I.2    Engelman, D.M.3
  • 35
    • 0028235050 scopus 로고
    • Specificity and promiscuity in membrane helix interactions
    • M.A. Lemmon, and D.M. Engelman Specificity and promiscuity in membrane helix interactions FEBS Lett. 346 1994 17 20
    • (1994) FEBS Lett. , vol.346 , pp. 17-20
    • Lemmon, M.A.1    Engelman, D.M.2
  • 36
    • 0026315513 scopus 로고
    • Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand
    • M.V. Milburn, G.G. Prive, D.L. Milligan, W.G. Scott, J. Yeh, J. Jancarik, D.E. Koshland Jr., and S.H. Kim Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand Science 254 1991 1342 1347
    • (1991) Science , vol.254 , pp. 1342-1347
    • Milburn, M.V.1    Prive, G.G.2    Milligan, D.L.3    Scott, W.G.4    Yeh, J.5    Jancarik, J.6    Koshland Jr., D.E.7    Kim, S.H.8
  • 37
    • 0029768644 scopus 로고    scopus 로고
    • Helix-helix interactions in lipid bilayers
    • N. Ben-Tal, and B. Honig Helix-helix interactions in lipid bilayers Biophys. J. 71 1996 3046 3050
    • (1996) Biophys. J. , vol.71 , pp. 3046-3050
    • Ben-Tal, N.1    Honig, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.