메뉴 건너뛰기




Volumn 37, Issue 1-2, 1997, Pages 74-83

Local electrostatic potentials in pyridoxal phosphate labelled horse heart cytochrome c

Author keywords

Electrostatic potentials; Molecular modelling; pH sensitive optical label; Pridoxal phosphate modified cytochrome c

Indexed keywords

CYTOCHROME C; HYDROXYL GROUP; PHENOL; PYRIDOXAL 5 PHOSPHATE;

EID: 0031035546     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1011-1344(96)07345-9     Document Type: Article
Times cited : (8)

References (48)
  • 1
    • 0018094892 scopus 로고
    • Electrostatic effects in proteins
    • [1] M.P. Perutz, Electrostatic effects in proteins, Science, 201 (1978) 1187-1191.
    • (1978) Science , vol.201 , pp. 1187-1191
    • Perutz, M.P.1
  • 2
    • 0000230329 scopus 로고
    • Energetics of enzyme catalysis
    • [2] A. Warshel, Energetics of enzyme catalysis, Proc. Natl. Acad. Sci. USA, 75 (1978) 5250-5254.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 5250-5254
    • Warshel, A.1
  • 3
    • 0020481290 scopus 로고
    • Analysis of electrostatic interactions and their relationship to conformation and stability of bovine pancreatic trypsin inhibitor
    • [3] K.L. March, D.G. Maskalik, R.D. England, S.H. Friend and F.R.N. Gurd, Analysis of electrostatic interactions and their relationship to conformation and stability of bovine pancreatic trypsin inhibitor, Biochemistry, 21 (1982) 5241-5251.
    • (1982) Biochemistry , vol.21 , pp. 5241-5251
    • March, K.L.1    Maskalik, D.G.2    England, R.D.3    Friend, S.H.4    Gurd, F.R.N.5
  • 4
    • 0022401765 scopus 로고
    • Electrostatic interactions in sperm whale myoglobin. Site specifity, roles in structural elements and external electrostatic potential distributions
    • [4] B.E. Garcia-Moreno, L.X. Chen, K.L. March, R.S. Gurd and F.R.N. Gurd, Electrostatic interactions in sperm whale myoglobin. Site specifity, roles in structural elements and external electrostatic potential distributions, J. Biol. Chem., 260 (1985) 14070-14082.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14070-14082
    • Garcia-Moreno, B.E.1    Chen, L.X.2    March, K.L.3    Gurd, R.S.4    Gurd, F.R.N.5
  • 5
    • 0025891413 scopus 로고
    • Electrostatic energy and macromolecular function
    • [5] A. Warshell and J. Aqvist, Electrostatic energy and macromolecular function, Ann. Rev. Biophys. Biophys. Chem., 20 (1991) 267-298.
    • (1991) Ann. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 267-298
    • Warshell, A.1    Aqvist, J.2
  • 6
    • 0025197061 scopus 로고
    • as of ionizable groups in proteins: Atomic detail from a continium electrostatic model
    • as of ionizable groups in proteins: atomic detail from a continium electrostatic model, Biochemistry, 29 (1990) 10219-10225.
    • (1990) Biochemistry , vol.29 , pp. 10219-10225
    • Bashford, D.1    Karplus, M.2
  • 7
    • 0028218956 scopus 로고
    • Environmental effects on the protonation states of active site residues in Bacteriorhodopsin
    • [7] R.V. Sampogna and B. Honig, Environmental effects on the protonation states of active site residues in Bacteriorhodopsin, Biophys. J., 66 (1994) 1341-1352.
    • (1994) Biophys. J. , vol.66 , pp. 1341-1352
    • Sampogna, R.V.1    Honig, B.2
  • 8
    • 0024396664 scopus 로고
    • Electrostatic interactions in proteins. A theoretical analysis of lysozyme ionization
    • [8] V.Z. Spassov, A.D. Karshikov and B.P. Atanasov, Electrostatic interactions in proteins. A theoretical analysis of lysozyme ionization, Biochim, Biophys. Acta, 999 (1989) 1-6.
    • (1989) Biochim, Biophys. Acta , vol.999 , pp. 1-6
    • Spassov, V.Z.1    Karshikov, A.D.2    Atanasov, B.P.3
  • 9
    • 0024802754 scopus 로고
    • Electrostatic interactions in proteins: Calculations of the electrostatic term of free energy and the electrostatic potential field
    • [9] A.D. Karshikov, R. Engh, W. Bode and B.P. Atanasov, Electrostatic interactions in proteins: Calculations of the electrostatic term of free energy and the electrostatic potential field, Eur. Biophys. J., 17 (1989) 287-297.
    • (1989) Eur. Biophys. J. , vol.17 , pp. 287-297
    • Karshikov, A.D.1    Engh, R.2    Bode, W.3    Atanasov, B.P.4
  • 10
    • 0019036697 scopus 로고
    • Electric potential at regions near the two specific thiols of heavy meromyosin determined by the fluorescence quenching techniques. I. Effect of ATP
    • [10] T. Ando, H. Fujisaki, K. Asai, Electric potential at regions near the two specific thiols of heavy meromyosin determined by the fluorescence quenching techniques. I. Effect of ATP, J. Biochem. (Tokyo), 88 (1980) 265-276.
    • (1980) J. Biochem. (Tokyo) , vol.88 , pp. 265-276
    • Ando, T.1    Fujisaki, H.2    Asai, K.3
  • 11
    • 0027119143 scopus 로고
    • Internal stark effect measurements of the electric field at the amino terminus of an α-helix
    • [11] D.J. Lockhart and P.S. Kim, Internal Stark effect measurements of the electric field at the amino terminus of an α-helix, Science, 257 (1992) 947-951.
    • (1992) Science , vol.257 , pp. 947-951
    • Lockhart, D.J.1    Kim, P.S.2
  • 12
    • 0024278385 scopus 로고
    • a shift of a fluorophore. 1. The 3′ terminus of 16 S RNA
    • a shift of a fluorophore. 1. The 3′ terminus of 16 S RNA, Eur. J. Biochem., 173 (1988) 227-231.
    • (1988) Eur. J. Biochem. , vol.173 , pp. 227-231
    • Friedrich, K.1    Woolley, P.2
  • 16
    • 0020064026 scopus 로고
    • Labeling of hemoglobin with pyridoxal phosphate
    • [16] R. Benesch, R.E. Benesch, and S. Kwong, Labeling of hemoglobin with pyridoxal phosphate, J. Biol. Chem., 257 (1982) 1320-1324.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1320-1324
    • Benesch, R.1    Benesch, R.E.2    Kwong, S.3
  • 18
    • 0023684587 scopus 로고
    • Evidence for the extramembranous location of the putative amphipathic helix of acetylcholine receptor
    • [18] B.P. Dwyer, Evidence for the extramembranous location of the putative amphipathic helix of acetylcholine receptor, Biochemistry, 27 (1988) 5586-5592.
    • (1988) Biochemistry , vol.27 , pp. 5586-5592
    • Dwyer, B.P.1
  • 19
    • 0024403725 scopus 로고
    • Pyridoxal phosphate as a probe of the cytoplasmic domains of transmembrane proteins: Application to the nicotinic acetylcholine receptor
    • [19] B. Perez-Ramirez and M. Martinez-Carrion, Pyridoxal phosphate as a probe of the cytoplasmic domains of transmembrane proteins: application to the nicotinic acetylcholine receptor, Biochemistry, 28 (1989) 5034-5040.
    • (1989) Biochemistry , vol.28 , pp. 5034-5040
    • Perez-Ramirez, B.1    Martinez-Carrion, M.2
  • 21
    • 0030008194 scopus 로고    scopus 로고
    • Characterization of pyridoxal phosphate as optical label for measuring electrostatic potentials in proteins
    • [21] G. Kossekova, M. Miteva and B. Atanasov, Characterization of pyridoxal phosphate as optical label for measuring electrostatic potentials in proteins, J. Photochem. Photobiol. B: Biol., 32 (1996) 71-79.
    • (1996) J. Photochem. Photobiol. B: Biol. , vol.32 , pp. 71-79
    • Kossekova, G.1    Miteva, M.2    Atanasov, B.3
  • 22
    • 0027056273 scopus 로고
    • Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c
    • [22] H. Pelletier and J. Kraut, Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c, Science, 258 (1992) 1748-1755.
    • (1992) Science , vol.258 , pp. 1748-1755
    • Pelletier, H.1    Kraut, J.2
  • 23
    • 0025007598 scopus 로고
    • High-resolution three-dimensional structure of horse heart cytochrome c
    • [23] G.W. Bushnell, G.V. Louie and G.D. Brayer, High-resolution three-dimensional structure of horse heart cytochrome c, J. Mol. Biol., 214 (1990) 1-14.
    • (1990) J. Mol. Biol. , vol.214 , pp. 1-14
    • Bushnell, G.W.1    Louie, G.V.2    Brayer, G.D.3
  • 24
    • 0021114740 scopus 로고
    • Penetration of small molecules into proteins studied by quenching of phosphorescence and fluorescence
    • [24] D.B. Calhoun, J.M. Vanderkooi and S.W. Englander, Penetration of small molecules into proteins studied by quenching of phosphorescence and fluorescence, Biochemistry, 22 (1983) 1533-1539.
    • (1983) Biochemistry , vol.22 , pp. 1533-1539
    • Calhoun, D.B.1    Vanderkooi, J.M.2    Englander, S.W.3
  • 25
    • 33847682952 scopus 로고
    • Correction of fluorescence spectra and measurement of fluorescence quantum efficiency
    • [25] C.A. Parker and W.T. Rees, Correction of fluorescence spectra and measurement of fluorescence quantum efficiency, Analyst, 85 (1960) 587-600.
    • (1960) Analyst , vol.85 , pp. 587-600
    • Parker, C.A.1    Rees, W.T.2
  • 26
    • 0001261908 scopus 로고
    • Measurement of absolute quantum efficiences of fluorescence
    • [26] W.H. Melhuish, Measurement of absolute quantum efficiences of fluorescence, N. Z. J. Sci Technol., 37B (1955) 142-149.
    • (1955) N. Z. J. Sci Technol. , vol.37 B , pp. 142-149
    • Melhuish, W.H.1
  • 28
    • 0026751404 scopus 로고
    • X-Ray structure refinement and comparison of three forms of mitochondrial aspartate amino transferase
    • [28] C. A. McPhalen, M.G. Vincent and J.N. Jansonius, X-Ray structure refinement and comparison of three forms of mitochondrial aspartate amino transferase, J. Mol. Biol., 225 (1992) 495-517.
    • (1992) J. Mol. Biol. , vol.225 , pp. 495-517
    • McPhalen, C.A.1    Vincent, M.G.2    Jansonius, J.N.3
  • 29
    • 0011330077 scopus 로고
    • The Cambridge structural database in molecular graphics tecniques for the rapid identification of conformational minima
    • [29] R. Taylor, The Cambridge structural database in molecular graphics tecniques for the rapid identification of conformational minima, J. Mol. Graphics, 4 (1986) 123-131.
    • (1986) J. Mol. Graphics , vol.4 , pp. 123-131
    • Taylor, R.1
  • 30
    • 84988129057 scopus 로고
    • Optimization of parameters for semiempirical methods. I method
    • [30] J.J.P. Stewart, Optimization of parameters for semiempirical methods. I Method, J. Comput. Chem., 10 (1989) 209-220.
    • (1989) J. Comput. Chem. , vol.10 , pp. 209-220
    • Stewart, J.J.P.1
  • 31
    • 0003977895 scopus 로고
    • [31] Biosym Technologies Inc., User Guide, 1992.
    • (1992) User Guide
  • 32
    • 0016399124 scopus 로고
    • Energy functions for peptides and proteins. I. Derivation of a consistent force field including the hydrogen bond from amide crystals
    • [32] A.T. Hagler, E. Huler and S. Lìfson, Energy functions for peptides and proteins. I. Derivation of a consistent force field including the hydrogen bond from amide crystals, J. Am. Chem. Soc., 96 (1974) 5319-5327.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 5319-5327
    • Hagler, A.T.1    Huler, E.2    Lìfson, S.3
  • 33
    • 0016399126 scopus 로고
    • Energy functions for peptides and proteins. II. Amide hydrogen bond and calculation of amide crystal properties
    • [33] A.T. Hagler and S. Lifson, Energy functions for peptides and proteins. II. Amide hydrogen bond and calculation of amide crystal properties, J. Am. Chem. Soc., 96 (1974) 5327-5335.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 5327-5335
    • Hagler, A.T.1    Lifson, S.2
  • 35
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • [35] B. Lee and F.M. Richards, The interpretation of protein structures: estimation of static accessibility, J. Mol. Biol., 55 (1971) 379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 36
    • 33947468892 scopus 로고
    • Theory of protein titration curves. I. General equation for impenetrable spheres
    • [36] C. Tanford and J.G. Kirkwood, Theory of protein titration curves. I. General equation for impenetrable spheres, J. Am. Chem. Soc., 79 (1957) 5333-5339.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 5333-5339
    • Tanford, C.1    Kirkwood, J.G.2
  • 38
    • 0005388526 scopus 로고
    • Acid-base properties of electronically excited states of organic molecules
    • [38] J.F. Ireland and P.A. Wyatt, Acid-base properties of electronically excited states of organic molecules, Adv. Phys. Org. Chem., 12 (1976) 131-221.
    • (1976) Adv. Phys. Org. Chem. , vol.12 , pp. 131-221
    • Ireland, J.F.1    Wyatt, P.A.2
  • 40
    • 85005670732 scopus 로고
    • Femtosecond-picosecond laser photolysis studies on proton transfer process of excited 1 pyrenol-triethylamine hydrogen bonding complex in solutions
    • [40] H. Miyasaka, K. Wada, S. Ojima and N. Mataga, Femtosecond-picosecond laser photolysis studies on proton transfer process of excited 1 pyrenol-triethylamine hydrogen bonding complex in solutions, Israel J. Chem., 33 (1993) 183-192.
    • (1993) Israel J. Chem. , vol.33 , pp. 183-192
    • Miyasaka, H.1    Wada, K.2    Ojima, S.3    Mataga, N.4
  • 41
    • 0000977244 scopus 로고
    • Proton transfer reaction rate as a probe of size-dependent properties of large water clusters
    • [41] R. Knohenmuss, G.R. Holtom and D. Ray, Proton transfer reaction rate as a probe of size-dependent properties of large water clusters, Chem. Phys. Lett., 215 (1993) 188-192.
    • (1993) Chem. Phys. Lett. , vol.215 , pp. 188-192
    • Knohenmuss, R.1    Holtom, G.R.2    Ray, D.3
  • 44
    • 0017651393 scopus 로고
    • Use of specific lysine modifications to locate the reaction site of cwtochrome c with cytochrome oxidase
    • [44] H.T. Smith, N. Staudenmayer and F. Millett, Use of specific lysine modifications to locate the reaction site of cwtochrome c with cytochrome oxidase, Biochemistry, 16 (1977) 4971-4974.
    • (1977) Biochemistry , vol.16 , pp. 4971-4974
    • Smith, H.T.1    Staudenmayer, N.2    Millett, F.3
  • 45
    • 0019321512 scopus 로고
    • Definition of enzymatic interaction domains on cytochrome c. 6. Purification and activity of singly substituted carboxydinitrophenyl-lysine 7, 25, 73, 86 and 99 cytochromes c
    • [45] N. Osheroff, D.L. Brautigan and E. Margoliash, Definition of enzymatic interaction domains on cytochrome c. 6. Purification and activity of singly substituted carboxydinitrophenyl-lysine 7, 25, 73, 86 and 99 cytochromes c, J. Biol Chem., 255 (1980) 8245-8251.
    • (1980) J. Biol Chem. , vol.255 , pp. 8245-8251
    • Osheroff, N.1    Brautigan, D.L.2    Margoliash, E.3
  • 46
    • 0018185853 scopus 로고
    • The cytochrome c oxidase binding site on cytochrome c. Differential chemical modification of lysine residues in free and oxidase-bound cytochrome
    • [46] R. Rieder and H.R. Bosshard, The cytochrome c oxidase binding site on cytochrome c. Differential chemical modification of lysine residues in free and oxidase-bound cytochrome, J. Biol. Chem., 253 (1978) 6045-6053
    • (1978) J. Biol. Chem. , vol.253 , pp. 6045-6053
    • Rieder, R.1    Bosshard, H.R.2
  • 47
    • 0020709955 scopus 로고
    • Identification of specific carboxylate groups on cytochrome c oxidase that are involved in binding cytochrome c
    • [47] F. Millett, C. De Jong, L. Paulson and R.A. Capaldi, Identification of specific carboxylate groups on cytochrome c oxidase that are involved in binding cytochrome c, Biochemistry, 22 (1983) 546-552.
    • (1983) Biochemistry , vol.22 , pp. 546-552
    • Millett, F.1    De Jong, C.2    Paulson, L.3    Capaldi, R.A.4
  • 48
    • 0024450107 scopus 로고
    • Ionic-strength-dependence of the oxidation of native and pyridoxal-5′-phosphate-modified cytochromes c by cytochrome c oxidase
    • [48] G. Kossekova, B. Atanasov, R. Bolli and A. Azzi, Ionic-strength-dependence of the oxidation of native and pyridoxal-5′-phosphate-modified cytochromes c by cytochrome c oxidase, Biochem. J., 262 (1989) 591-596.
    • (1989) Biochem. J. , vol.262 , pp. 591-596
    • Kossekova, G.1    Atanasov, B.2    Bolli, R.3    Azzi, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.