메뉴 건너뛰기




Volumn 102, Issue 3, 2012, Pages 579-586

Comprehensive determination of protein tyrosine pK a values for photoactive yellow protein using indirect 13C NMR spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PHOTOACTIVE YELLOW PROTEIN, BACTERIA; PROTON; TYROSINE; VISUAL PROTEINS AND PIGMENTS;

EID: 84856716175     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.12.024     Document Type: Article
Times cited : (16)

References (43)
  • 1
    • 0027324441 scopus 로고
    • The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein
    • W.W. Sprenger, and W.D. Hoff K.J. Hellingwerf The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein J. Bacteriol. 175 1993 3096 3104 (Pubitemid 23148746)
    • (1993) Journal of Bacteriology , vol.175 , Issue.10 , pp. 3096-3104
    • Sprenger, W.W.1    Hoff, W.D.2    Armitage, J.P.3    Hellingwerf, K.J.4
  • 2
    • 0032568630 scopus 로고    scopus 로고
    • Photoactive yellow protein: A structural prototype for the three-dimensional fold of the PAS domain superfamily
    • J.L. Pellequer, and K.A. Wager-Smith E.D. Getzoff Photoactive yellow protein: a structural prototype for the three-dimensional fold of the PAS domain superfamily Proc. Natl. Acad. Sci. USA 95 1998 5884 5890
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5884-5890
    • Pellequer, J.L.1    Wager-Smith, K.A.2    Getzoff, E.D.3
  • 3
    • 0029110488 scopus 로고
    • 1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore
    • G.E. Borgstahl, D.R. Williams, and E.D. Getzoff 1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore Biochemistry 34 1995 6278 6287
    • (1995) Biochemistry , vol.34 , pp. 6278-6287
    • Borgstahl, G.E.1    Williams, D.R.2    Getzoff, E.D.3
  • 7
    • 67249133227 scopus 로고    scopus 로고
    • Hydrogen bond dynamics in the active site of photoactive yellow protein
    • P.A. Sigala, M.A. Tsuchida, and D. Herschlag Hydrogen bond dynamics in the active site of photoactive yellow protein Proc. Natl. Acad. Sci. USA 106 2009 9232 9237
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 9232-9237
    • Sigala, P.A.1    Tsuchida, M.A.2    Herschlag, D.3
  • 8
    • 0034619501 scopus 로고    scopus 로고
    • Coupling of hydrogen bonding to chromophore conformation and function in photoactive yellow protein
    • R. Brudler, and T.E. Meyer E.D. Getzoff Coupling of hydrogen bonding to chromophore conformation and function in photoactive yellow protein Biochemistry 39 2000 13478 13486
    • (2000) Biochemistry , vol.39 , pp. 13478-13486
    • Brudler, R.1    Meyer, T.E.2    Getzoff, E.D.3
  • 9
    • 34247899119 scopus 로고    scopus 로고
    • Structure and photoreaction of photoactive yellow protein, a structural prototype of the PAS domain superfamily
    • DOI 10.1562/2006-02-28-IR-827
    • Y. Imamoto, and M. Kataoka Structure and photoreaction of photoactive yellow protein, a structural prototype of the PAS domain superfamily Photochem. Photobiol. 83 2007 40 49 (Pubitemid 46697222)
    • (2007) Photochemistry and Photobiology , vol.83 , Issue.1 , pp. 40-49
    • Imamoto, Y.1    Kataoka, M.2
  • 11
    • 0030446427 scopus 로고    scopus 로고
    • Glu46 donates a proton to the 4-hydroxycinnamate anion chromophore during the photocycle of photoactive yellow protein
    • DOI 10.1021/bi9623035
    • A. Xie, and W.D. Hoff K.J. Hellingwerf Glu46 donates a proton to the 4-hydroxycinnamate anion chromophore during the photocycle of photoactive yellow protein Biochemistry 35 1996 14671 14678 (Pubitemid 26423797)
    • (1996) Biochemistry , vol.35 , Issue.47 , pp. 14671-14678
    • Xie, A.1    Hoff, W.D.2    Kroon, A.R.3    Hellingwerf, K.J.4
  • 12
    • 77957919296 scopus 로고    scopus 로고
    • Subpicosecond excited-state proton transfer preceding isomerization during the photorecovery of photoactive yellow protein
    • E.C. Carroll, and S.H. Song D.S. Larsen Subpicosecond excited-state proton transfer preceding isomerization during the photorecovery of photoactive yellow protein J Phys Chem Lett. 1 2010 2793 2799
    • (2010) J Phys Chem Lett. , vol.1 , pp. 2793-2799
    • Carroll, E.C.1    Song, S.H.2    Larsen, D.S.3
  • 13
    • 0031808072 scopus 로고    scopus 로고
    • New photocycle intermediates in the photoactive yellow protein from Ectothiorhodospira halophila: Picosecond transient absorption spectroscopy
    • L. Ujj, and S. Devanathan G.H. Atkinson New photocycle intermediates in the photoactive yellow protein from Ectothiorhodospira halophila: picosecond transient absorption spectroscopy Biophys. J. 75 1998 406 412 (Pubitemid 28311827)
    • (1998) Biophysical Journal , vol.75 , Issue.1 , pp. 406-412
    • Ujj, L.1    Devanathan, S.2    Meyer, T.E.3    Cusanovich, M.A.4    Tollin, G.5    Atkinson, G.H.6
  • 15
    • 0035906913 scopus 로고    scopus 로고
    • The role of the N-terminal domain of photoactive yellow protein in the transient partial unfolding during signalling state formation
    • DOI 10.1016/S0014-5793(01)02427-9, PII S0014579301024279
    • M.A. van der Horst, and I.H. van Stokkum K.J. Hellingwerf The role of the N-terminal domain of photoactive yellow protein in the transient partial unfolding during signalling state formation FEBS Lett. 497 2001 26 30 (Pubitemid 32480175)
    • (2001) FEBS Letters , vol.497 , Issue.1 , pp. 26-30
    • Van Der Horst, M.A.1    Van Stokkum, I.H.2    Crielaard, W.3    Hellingwerf, K.J.4
  • 16
    • 64149111644 scopus 로고    scopus 로고
    • PH Dependence of the photoactive yellow protein photocycle recovery reaction reveals a new late photocycle intermediate with a deprotonated chromophore
    • J. Hendriks, and K.J. Hellingwerf pH Dependence of the photoactive yellow protein photocycle recovery reaction reveals a new late photocycle intermediate with a deprotonated chromophore J. Biol. Chem. 284 2009 5277 5288
    • (2009) J. Biol. Chem. , vol.284 , pp. 5277-5288
    • Hendriks, J.1    Hellingwerf, K.J.2
  • 17
    • 7544223280 scopus 로고    scopus 로고
    • Direct observation of the pH-dependent equilibrium between L-like and M intermediates of photoactive yellow protein
    • DOI 10.1016/j.febslet.2004.09.065, PII S0014579304011986
    • Y. Imamoto, M. Harigai, and M. Kataoka Direct observation of the pH-dependent equilibrium between L-like and M intermediates of photoactive yellow protein FEBS Lett. 577 2004 75 80 (Pubitemid 39452363)
    • (2004) FEBS Letters , vol.577 , Issue.1-2 , pp. 75-80
    • Imamoto, Y.1    Harigai, M.2    Kataoka, M.3
  • 18
    • 0015937171 scopus 로고
    • A nuclear magnetic resonance study of bovine pancreatic trypsin inhibitor. Tyrosine titrations and backbone NH groups
    • S. Karplus, G.H. Snyder, and B.D. Sykes A nuclear magnetic resonance study of bovine pancreatic trypsin inhibitor. Tyrosine titrations and backbone NH groups Biochemistry 12 1973 1323 1329
    • (1973) Biochemistry , vol.12 , pp. 1323-1329
    • Karplus, S.1    Snyder, G.H.2    Sykes, B.D.3
  • 19
    • 37049140963 scopus 로고
    • Carbon-13 nuclear magnetic resonance study of tyrosine titrations
    • R. Norton, and J. Bradbury Carbon-13 nuclear magnetic resonance study of tyrosine titrations J. Chem. Soc. Chem. Commun. 21 1974 870 871
    • (1974) J. Chem. Soc. Chem. Commun. , vol.21 , pp. 870-871
    • Norton, R.1    Bradbury, J.2
  • 20
    • 0037391280 scopus 로고    scopus 로고
    • a measurements from nuclear magnetic resonance of tyrosine-150 in class C β-lactamase
    • DOI 10.1042/BJ20021447
    • a measurements from nuclear magnetic resonance of tyrosine-150 in class C β-lactamase Biochem. J. 371 2003 175 181 (Pubitemid 36458091)
    • (2003) Biochemical Journal , vol.371 , Issue.1 , pp. 175-181
    • Kato-Toma, Y.1    Iwashita, T.2    Masuda, K.3    Oyama, Y.4    Ishiguro, M.5
  • 21
    • 0017593560 scopus 로고
    • Tyrosine emission in the tryptophanless azurin from Pseudomonas fluorescens
    • K. Ugurbil, and R. Bersohn Tyrosine emission in the tryptophanless azurin from Pseudomonas fluorescens Biochemistry 16 1977 895 901 (Pubitemid 8054872)
    • (1977) Biochemistry , vol.16 , Issue.5 , pp. 895-901
    • Ugurbil, K.1    Bersohn, R.2
  • 22
    • 0017144777 scopus 로고
    • Titration behavior of individual tyrosine residues of myoglobins from sperm whale, horse, and red kangaroo
    • D.J. Wilbur, and A. Allerhand Titration behavior of individual tyrosine residues of myoglobins from sperm whale, horse, and red kangaroo J. Biol. Chem. 251 1976 5187 5194
    • (1976) J. Biol. Chem. , vol.251 , pp. 5187-5194
    • Wilbur, D.J.1    Allerhand, A.2
  • 25
    • 0028232021 scopus 로고
    • Individual ionization constants of all the carboxyl groups in ribonuclease HI from Escherichia coli determined by NMR
    • DOI 10.1021/bi00183a034
    • Y. Oda, and T. Yamazaki H. Nakamura Individual ionization constants of all the carboxyl groups in ribonuclease HI from Escherichia coli determined by NMR Biochemistry 33 1994 5275 5284 (Pubitemid 24150996)
    • (1994) Biochemistry , vol.33 , Issue.17 , pp. 5275-5284
    • Oda, Y.1    Yamazaki, T.2    Nagayama, K.3    Kanaya, S.4    Kuroda, Y.5    Nakamura, H.6
  • 26
    • 80755140499 scopus 로고    scopus 로고
    • Structure, dynamics, and ionization equilibria of the tyrosine residues in Bacillus circulans xylanase
    • S.J. Baturin, M. Okon, and L.P. McIntosh Structure, dynamics, and ionization equilibria of the tyrosine residues in Bacillus circulans xylanase J. Biomol. NMR 51 2011 379 394
    • (2011) J. Biomol. NMR , vol.51 , pp. 379-394
    • Baturin, S.J.1    Okon, M.2    McIntosh, L.P.3
  • 27
    • 70349731658 scopus 로고    scopus 로고
    • Hydrogen bonding controls excited-state decay of the photoactive yellow protein chromophore
    • M. Boggio-Pasqua, M.A. Robb, and G. Groenhof Hydrogen bonding controls excited-state decay of the photoactive yellow protein chromophore J. Am. Chem. Soc. 131 2009 13580 13581
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 13580-13581
    • Boggio-Pasqua, M.1    Robb, M.A.2    Groenhof, G.3
  • 29
    • 73249126534 scopus 로고    scopus 로고
    • Hydrogen exchange rate of tyrosine hydroxyl groups in proteins as studied by the deuterium isotope effect on C(ζ) chemical shifts
    • M. Takeda, and J. Jee M. Kainosho Hydrogen exchange rate of tyrosine hydroxyl groups in proteins as studied by the deuterium isotope effect on C(ζ) chemical shifts J. Am. Chem. Soc. 131 2009 18556 18562
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 18556-18562
    • Takeda, M.1    Jee, J.2    Kainosho, M.3
  • 31
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • F. Delaglio, and S. Grzesiek A. Bax NMRPipe: a multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6 1995 277 293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Bax, A.3
  • 32
    • 0004040543 scopus 로고    scopus 로고
    • University of California San Francisco
    • T. Goddard, and D. Kneller SPARKY 3 2004 University of California San Francisco
    • (2004) SPARKY 3
    • Goddard, T.1    Kneller, D.2
  • 33
    • 0032528988 scopus 로고    scopus 로고
    • Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB inter-union task group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy
    • J.L. Markley, and A. Bax K. Wüthrich Recommendations for the presentation of NMR structures of proteins and nucleic acids-IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy Eur. J. Biochem. 256 1998 1 15 (Pubitemid 28399089)
    • (1998) European Journal of Biochemistry , vol.256 , Issue.1 , pp. 1-15
    • Markley, J.L.1    Bax, A.2    Arata, Y.3    Hilbers, C.W.4    Kaptein, R.5    Sykes, B.D.6    Wright, P.E.7    Wuthrich, K.8
  • 34
    • 79952441586 scopus 로고    scopus 로고
    • 100% complete assignment of non-labile (1)H, (13)C, and (15)N signals for calcium-loaded Calbindin D(9k) P43G
    • N.A. Oktaviani, and R. Otten F.A.A. Mulder 100% complete assignment of non-labile (1)H, (13)C, and (15)N signals for calcium-loaded Calbindin D(9k) P43G Biomol. NMR Assign. 5 2011 79 84
    • (2011) Biomol. NMR Assign. , vol.5 , pp. 79-84
    • Oktaviani, N.A.1    Otten, R.2    Mulder, F.A.A.3
  • 38
    • 79551502607 scopus 로고    scopus 로고
    • Remeasuring HEWL pK(a) values by NMR spectroscopy: Methods, analysis, accuracy, and implications for theoretical pK(a) calculations
    • H. Webb, and B.M. Tynan-Connolly J.E. Nielsen Remeasuring HEWL pK(a) values by NMR spectroscopy: methods, analysis, accuracy, and implications for theoretical pK(a) calculations Proteins 79 2011 685 702
    • (2011) Proteins , vol.79 , pp. 685-702
    • Webb, H.1    Tynan-Connolly, B.M.2    Nielsen, J.E.3
  • 39
    • 0036001159 scopus 로고    scopus 로고
    • a values of catalytic groups in enzyme active sites
    • DOI 10.1080/15216540211468
    • a values of catalytic groups in enzyme active sites IUBMB Life 53 2002 85 98 (Pubitemid 34553129)
    • (2002) IUBMB Life , vol.53 , Issue.2 , pp. 85-98
    • Harris, T.K.1    Turner, G.J.2
  • 40
    • 0034727659 scopus 로고    scopus 로고
    • Probing the nature of the blue-shifted intermediate of photoactive yellow protein in solution by NMR: Hydrogen-deuterium exchange data and pH studies
    • C.J. Craven, and N.M. Derix R. Kaptein Probing the nature of the blue-shifted intermediate of photoactive yellow protein in solution by NMR: hydrogen-deuterium exchange data and pH studies Biochemistry 39 2000 14392 14399
    • (2000) Biochemistry , vol.39 , pp. 14392-14399
    • Craven, C.J.1    Derix, N.M.2    Kaptein, R.3
  • 41
    • 0030069979 scopus 로고    scopus 로고
    • Chemical reactivity and spectroscopy of the thiol ester-linked p-coumaric acid chromophore in the photoactive yellow protein from Ectothiorhodospira halophila
    • DOI 10.1021/bi951755z
    • W.D. Hoff, and B. Devreese K.J. Hellingwerf Chemical reactivity and spectroscopy of the thiol ester-linked p-coumaric acid chromophore in the photoactive yellow protein from Ectothiorhodospira halophila Biochemistry 35 1996 1274 1281 (Pubitemid 26050791)
    • (1996) Biochemistry , vol.35 , Issue.4 , pp. 1274-1281
    • Hoff, W.D.1    Devreese, B.2    Fokkens, R.3    Nugteren-Roodzant, I.M.4    Van Beeumen, J.5    Nibbering, N.6    Hellingwerf, K.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.