메뉴 건너뛰기




Volumn 1777, Issue 4, 2008, Pages 362-368

Inhibition of the ATPase activity of the catalytic portion of ATP synthases by cationic amphiphiles

Author keywords

ATPase activity; Cationic detergent; Chloroplast ATP synthase; Melittin; Subunit dissociation

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATASE (MAGNESIUM); AMPHOPHILE; CETRIMIDE; MELITTIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 40949158758     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2008.01.010     Document Type: Article
Times cited : (19)

References (36)
  • 1
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase-A splendid molecular machine
    • Boyer P.D. The ATP synthase-A splendid molecular machine. Annu. Rev. Biochem. 66 (1997) 717-749
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 2
    • 0000228422 scopus 로고
    • A soluble heat stable protein in mitochondria from bovine heart that inhibits ATP hydrolase activity
    • Pullman M.E., and Monroy G.C. A soluble heat stable protein in mitochondria from bovine heart that inhibits ATP hydrolase activity. J. Biol. Chem. 238 (1963) 3762-3769
    • (1963) J. Biol. Chem. , vol.238 , pp. 3762-3769
    • Pullman, M.E.1    Monroy, G.C.2
  • 3
    • 0017351393 scopus 로고
    • Purification of membrane attachment and inhibitory subunits of proton-translocating adenosine triphosphatase from Escherichia coli
    • Smith J.B., and Sternweis P.C. Purification of membrane attachment and inhibitory subunits of proton-translocating adenosine triphosphatase from Escherichia coli. Biochemistry 16 (1979) 306-311
    • (1979) Biochemistry , vol.16 , pp. 306-311
    • Smith, J.B.1    Sternweis, P.C.2
  • 4
    • 0021770639 scopus 로고
    • Preparation of the ε subunit and ε subunit deficient chloroplast coupling factor 1 in reconstitutively active forms
    • Richter M.L., Patrie W.D., and McCarty R.E. Preparation of the ε subunit and ε subunit deficient chloroplast coupling factor 1 in reconstitutively active forms. J. Biol. Chem. 259 (1984) 7371-7373
    • (1984) J. Biol. Chem. , vol.259 , pp. 7371-7373
    • Richter, M.L.1    Patrie, W.D.2    McCarty, R.E.3
  • 5
    • 0021759532 scopus 로고
    • Role of the gamma-subunit of chloroplast coupling factor I in the light-dependent activation of photophosphorylation and ATPase activity by dithiothreitol
    • R Ketcham S., Davenport J.W., Warncke K., and McCarty R.E. Role of the gamma-subunit of chloroplast coupling factor I in the light-dependent activation of photophosphorylation and ATPase activity by dithiothreitol. J. Biol. Chem. 259 (1984) 7286-7293
    • (1984) J. Biol. Chem. , vol.259 , pp. 7286-7293
    • R Ketcham, S.1    Davenport, J.W.2    Warncke, K.3    McCarty, R.E.4
  • 6
    • 0025213388 scopus 로고
    • The dithiothreitol-stimulated dissociation of the chloroplast coupling factor-1 epsilon subunit is reversible
    • Duhe R.J., and Selman B.R. The dithiothreitol-stimulated dissociation of the chloroplast coupling factor-1 epsilon subunit is reversible. Biochim. Biophys. Acta 1017 (1990) 70-78
    • (1990) Biochim. Biophys. Acta , vol.1017 , pp. 70-78
    • Duhe, R.J.1    Selman, B.R.2
  • 7
    • 0033623349 scopus 로고    scopus 로고
    • Structure of the γ-ε complex of ATP synthase
    • Rodgers A.J., and Wilce M.C. Structure of the γ-ε complex of ATP synthase. Nat. Struct. Biol. 7 (2000) 1051-1054
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1051-1054
    • Rodgers, A.J.1    Wilce, M.C.2
  • 8
    • 0037168499 scopus 로고    scopus 로고
    • The C-terminal domain of the chloroplast ATP synthase is not required for ATP synthesis
    • Nowak K.F., Tabidze V., and McCarty R.E. The C-terminal domain of the chloroplast ATP synthase is not required for ATP synthesis. Biochemistry 41 (2002) 15130-15134
    • (2002) Biochemistry , vol.41 , pp. 15130-15134
    • Nowak, K.F.1    Tabidze, V.2    McCarty, R.E.3
  • 9
    • 1542743652 scopus 로고    scopus 로고
    • Regulatory role of the C-Terminus of the ε subunit from the chloroplast ATP synthase
    • Nowak K.F., and McCarty R.E. Regulatory role of the C-Terminus of the ε subunit from the chloroplast ATP synthase. Biochemistry 43 (2004) 3273-3279
    • (2004) Biochemistry , vol.43 , pp. 3273-3279
    • Nowak, K.F.1    McCarty, R.E.2
  • 12
    • 15944371520 scopus 로고    scopus 로고
    • 1-ATPase from bovine heart mitochondria
    • 1-ATPase from bovine heart mitochondria. Biochem. J. 386 (2005) 591-598
    • (2005) Biochem. J. , vol.386 , pp. 591-598
    • Gledhill, J.R.1    Walker, J.E.2
  • 13
    • 0019627926 scopus 로고
    • Melittin inhibition and uncoupling of spinach thylakoids
    • Davis G.E., and Berg S.P. Melittin inhibition and uncoupling of spinach thylakoids. Arch. Biochem. Biophys. 221 (1981) 297-304
    • (1981) Arch. Biochem. Biophys. , vol.221 , pp. 297-304
    • Davis, G.E.1    Berg, S.P.2
  • 14
    • 0014878191 scopus 로고
    • Effect of hydrocarbon chain length on the uncoupling of photophosphorylation by amines
    • McCarty R.E., and Coleman C.H. Effect of hydrocarbon chain length on the uncoupling of photophosphorylation by amines. Arch. Biochem. Biophys. 141 (1970) 198-206
    • (1970) Arch. Biochem. Biophys. , vol.141 , pp. 198-206
    • McCarty, R.E.1    Coleman, C.H.2
  • 15
    • 0017368370 scopus 로고
    • Reversible binding of Pi by beef-heart mitochondrial adenosine triphophatase
    • Penefsky H.S. Reversible binding of Pi by beef-heart mitochondrial adenosine triphophatase. J. Biol. Chem. 252 (1977) 2091-2099
    • (1977) J. Biol. Chem. , vol.252 , pp. 2091-2099
    • Penefsky, H.S.1
  • 16
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding
    • Bradford M.M. Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-252
    • (1976) Anal. Biochem. , vol.72 , pp. 248-252
    • Bradford, M.M.1
  • 17
    • 3342922088 scopus 로고
    • A microcolorimetric method for the determination of inorganic phosphate
    • Taussky H.H., and Shorr E. A microcolorimetric method for the determination of inorganic phosphate. J. Biol. Chem. 202 (1953) 675-685
    • (1953) J. Biol. Chem. , vol.202 , pp. 675-685
    • Taussky, H.H.1    Shorr, E.2
  • 18
    • 0022625326 scopus 로고
    • Determination of the critical micelle concentration of surfactants using the fluorescent probe N-phenyl-1-naphthlamine
    • Brito R.M.M., and Vaz W.L.C. Determination of the critical micelle concentration of surfactants using the fluorescent probe N-phenyl-1-naphthlamine. Anal. Biochem. 152 (1986) 250-255
    • (1986) Anal. Biochem. , vol.152 , pp. 250-255
    • Brito, R.M.M.1    Vaz, W.L.C.2
  • 19
    • 0014286030 scopus 로고
    • A rapid, sensitive spectrophotometric method for the determination of sulfatides
    • Keen E.L. A rapid, sensitive spectrophotometric method for the determination of sulfatides. J. Lipid Res. 9 (1968) 319-327
    • (1968) J. Lipid Res. , vol.9 , pp. 319-327
    • Keen, E.L.1
  • 20
    • 0018959292 scopus 로고
    • Calcium-induced exposure of a hydrophobic surface on calmodulin
    • LaPorte D.C., Wierman B.M., and Storm D.R. Calcium-induced exposure of a hydrophobic surface on calmodulin. Biochemistry 19 (1980) 3814-3819
    • (1980) Biochemistry , vol.19 , pp. 3814-3819
    • LaPorte, D.C.1    Wierman, B.M.2    Storm, D.R.3
  • 21
    • 0014342841 scopus 로고
    • Quantitative estimation of protein binding site polarity. Fluorescence of N-arylaminonaphthalenesulfonates
    • Turner D.C., and Brand L. Quantitative estimation of protein binding site polarity. Fluorescence of N-arylaminonaphthalenesulfonates. Biochemistry 7 (1968) 3381-3390
    • (1968) Biochemistry , vol.7 , pp. 3381-3390
    • Turner, D.C.1    Brand, L.2
  • 22
    • 0002166785 scopus 로고
    • Sulfite stimulation of chloroplast coupling factor ATPase
    • Larson E.M., and Jagendorf A.T. Sulfite stimulation of chloroplast coupling factor ATPase. Biochim. Biophys. Acta 973 (1989) 67-77
    • (1989) Biochim. Biophys. Acta , vol.973 , pp. 67-77
    • Larson, E.M.1    Jagendorf, A.T.2
  • 23
    • 0026697590 scopus 로고
    • Modifications of the gamma-subunit of chloroplast coupling factor-I alter interactions with the inhibitory epsilon-subunit
    • Soteropoulos P., Suess K.H., and McCarty R.E. Modifications of the gamma-subunit of chloroplast coupling factor-I alter interactions with the inhibitory epsilon-subunit. J. Biol. Chem. 267 (1992) 10348-10354
    • (1992) J. Biol. Chem. , vol.267 , pp. 10348-10354
    • Soteropoulos, P.1    Suess, K.H.2    McCarty, R.E.3
  • 24
    • 0025213388 scopus 로고
    • The dithiothreitol-stimulated dissociation of the chloroplast coupling factor-1 epsilon-subunit is reversible
    • Duhe R.J., and Selman B.R. The dithiothreitol-stimulated dissociation of the chloroplast coupling factor-1 epsilon-subunit is reversible. Biochim. Biophys. Acta 1017 (1990) 70-78
    • (1990) Biochim. Biophys. Acta , vol.1017 , pp. 70-78
    • Duhe, R.J.1    Selman, B.R.2
  • 25
    • 0029942477 scopus 로고    scopus 로고
    • Proteolytic cleavage within a regulatory region of the gamma subunit of chloroplast coupling factor 1
    • Hightower K.E., and McCarty R.E. Proteolytic cleavage within a regulatory region of the gamma subunit of chloroplast coupling factor 1. Biochemistry 35 (1996) 4846-4851
    • (1996) Biochemistry , vol.35 , pp. 4846-4851
    • Hightower, K.E.1    McCarty, R.E.2
  • 26
    • 0032545250 scopus 로고    scopus 로고
    • Artificial chaperone-assisted refolding of citrate synthase
    • Daugherty D.L., Rozeman D., Hanson P.E., and Gellman S.H. Artificial chaperone-assisted refolding of citrate synthase. J. Biol. Chem. 273 (1998) 33961-33971
    • (1998) J. Biol. Chem. , vol.273 , pp. 33961-33971
    • Daugherty, D.L.1    Rozeman, D.2    Hanson, P.E.3    Gellman, S.H.4
  • 27
    • 0029757152 scopus 로고    scopus 로고
    • Influence of nucleotides on the cold stability of chloroplast coupling factor 1
    • Hightower K.E., and McCarty R.E. Influence of nucleotides on the cold stability of chloroplast coupling factor 1. Biochemistry 35 (1996) 10051-10057
    • (1996) Biochemistry , vol.35 , pp. 10051-10057
    • Hightower, K.E.1    McCarty, R.E.2
  • 28
    • 0021099728 scopus 로고
    • Conformational studies of aqueous melittin. Characteristics of a fluorescent probe binding site
    • Condie C.C., and Quay S.C. Conformational studies of aqueous melittin. Characteristics of a fluorescent probe binding site. J. Biol. Chem. 258 (1983) 8231-8234
    • (1983) J. Biol. Chem. , vol.258 , pp. 8231-8234
    • Condie, C.C.1    Quay, S.C.2
  • 29
    • 0020712137 scopus 로고
    • Conformational studies of aqueous melittin: thermodynamic parameters of the monomer-tetramer self-association reaction
    • Quay S.C., and Condie C.C. Conformational studies of aqueous melittin: thermodynamic parameters of the monomer-tetramer self-association reaction. Biochem. 22 (1983) 695-700
    • (1983) Biochem. , vol.22 , pp. 695-700
    • Quay, S.C.1    Condie, C.C.2
  • 32
    • 4243502126 scopus 로고
    • The relation of photosynthetic phosphorylation to the Hill reaction
    • Avron M., Krogman D.W., and Jagendorf A.T. The relation of photosynthetic phosphorylation to the Hill reaction. Biochim. Biophys. Acta 30 (1958) 144-153
    • (1958) Biochim. Biophys. Acta , vol.30 , pp. 144-153
    • Avron, M.1    Krogman, D.W.2    Jagendorf, A.T.3
  • 33
    • 9144260682 scopus 로고    scopus 로고
    • Observation of calcium-dependent unidirectional rotational motion in recombinant photosynthetic F1-ATPase molecules
    • Tucker W.C., Schwarz A., Levine T., Du Z., Gromet-Elhanan Z., Richter M.L., and Haran G. Observation of calcium-dependent unidirectional rotational motion in recombinant photosynthetic F1-ATPase molecules. J. Biol.Chem. 279 (2004) 47415-47418
    • (2004) J. Biol.Chem. , vol.279 , pp. 47415-47418
    • Tucker, W.C.1    Schwarz, A.2    Levine, T.3    Du, Z.4    Gromet-Elhanan, Z.5    Richter, M.L.6    Haran, G.7
  • 34
    • 0028867079 scopus 로고
    • +-ATPase (ATP synthase) is an essential residue for cooperative catalysis
    • +-ATPase (ATP synthase) is an essential residue for cooperative catalysis. J. Biol. Chem. 270 (1995) 25656-25660
    • (1995) J. Biol. Chem. , vol.270 , pp. 25656-25660
    • Omote, H.1    Le, N.P.2    Maeda, M.3    Futai, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.