메뉴 건너뛰기




Volumn 324, Issue 2, 2004, Pages 529-533

Ni 2+ binds to active site of hen egg-white lysozyme and quenches fluorescence of Trp62 and Trp108

Author keywords

Crystal structure; Lysozyme; Nickel (II) ion; Trp108; Trp62; Tryptophyl fluorescence

Indexed keywords

ACETIC ACID; EGG WHITE; LYSOZYME; NICKEL CHLORIDE; NITROGEN; TRYPTOPHAN; WATER; ASPARTIC ACID; ION; NICKEL; SODIUM CHLORIDE;

EID: 5144230465     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.09.078     Document Type: Article
Times cited : (15)

References (24)
  • 1
    • 0016312037 scopus 로고
    • The quenching of the tryptophyl and tyrosyl fluorescence of proteins by cesium ion
    • W. Altekar The quenching of the tryptophyl and tyrosyl fluorescence of proteins by cesium ion FEBS Lett. 49 1974 208 211
    • (1974) FEBS Lett. , vol.49 , pp. 208-211
    • Altekar, W.1
  • 2
    • 0017601167 scopus 로고
    • Fluorescence of proteins in aqueous neutral salt solutions. II. Influence of monovalent cation chlorides, particularly cesium chloride
    • W. Altekar Fluorescence of proteins in aqueous neutral salt solutions. II. Influence of monovalent cation chlorides, particularly cesium chloride Biopolymers 16 1977 369 386
    • (1977) Biopolymers , vol.16 , pp. 369-386
    • Altekar, W.1
  • 3
    • 0021755248 scopus 로고
    • Mechanism of protein salting in and salting out by divalent cation salts: Balance between hydration and salt binding
    • T. Arakawa, and S.N. Timasheff Mechanism of protein salting in and salting out by divalent cation salts: balance between hydration and salt binding Biochemistry 23 1984 5912 5923
    • (1984) Biochemistry , vol.23 , pp. 5912-5923
    • Arakawa, T.1    Timasheff, S.N.2
  • 4
    • 0024969402 scopus 로고
    • Relative effectiveness of various ions on the solubility and crystal growth of lysozyme
    • M. Riès-Kautt, and A.F. Ducruix Relative effectiveness of various ions on the solubility and crystal growth of lysozyme J. Biol. Chem. 264 1989 745 748
    • (1989) J. Biol. Chem. , vol.264 , pp. 745-748
    • Riès-Kautt, M.1    Ducruix, A.F.2
  • 5
    • 0031052836 scopus 로고    scopus 로고
    • Inferences drawn from physicochemical studies of crystallogenesis and precrystalline state
    • M. Riès-Kautt, and A. Ducruix Inferences drawn from physicochemical studies of crystallogenesis and precrystalline state Methods Enzymol. 276 1997 23 59
    • (1997) Methods Enzymol. , vol.276 , pp. 23-59
    • Riès-Kautt, M.1    Ducruix, A.2
  • 6
    • 0036794621 scopus 로고    scopus 로고
    • Strong and specific effects of cations on lysozyme chloride solubility
    • P. Bénas, L. Legrand, and M. Riès-Kautt Strong and specific effects of cations on lysozyme chloride solubility Acta Crystallogr. D 58 2002 1582 1587
    • (2002) Acta Crystallogr. D , vol.58 , pp. 1582-1587
    • Bénas, P.1    Legrand, L.2    Riès-Kautt, M.3
  • 9
    • 0015577933 scopus 로고
    • 2+ ions with hen egg-white lysozyme and with its N-acetylchitooligosaccharide complexes
    • 2+ ions with hen egg-white lysozyme and with its N-acetylchitooligosaccharide complexes J. Biochem. (Tokyo) 73 1973 307 322
    • (1973) J. Biochem. (Tokyo) , vol.73 , pp. 307-322
    • Ikeda, K.1    Hamaguchi, K.2
  • 10
    • 0016137153 scopus 로고
    • Binding of divalent copper ions to aspartic acid residue 52 in hen egg-white lysozyme
    • V.I. Teichberg, N. Sharon, J. Moult, A. Smilansky, and A. Yonath Binding of divalent copper ions to aspartic acid residue 52 in hen egg-white lysozyme J. Mol. Biol. 87 1974 368 375
    • (1974) J. Mol. Biol. , vol.87 , pp. 368-375
    • Teichberg, V.I.1    Sharon, N.2    Moult, J.3    Smilansky, A.4    Yonath, A.5
  • 11
    • 0016754338 scopus 로고
    • Metal ion binding in triclinic lysozyme
    • K. Kurachi, L.C. Sieker, and L.H. Jensen Metal ion binding in triclinic lysozyme J. Biol. Chem. 250 1975 7663 7667
    • (1975) J. Biol. Chem. , vol.250 , pp. 7663-7667
    • Kurachi, K.1    Sieker, L.C.2    Jensen, L.H.3
  • 12
    • 0000695363 scopus 로고    scopus 로고
    • High-resolution structure (1.33 Å) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from spaceHab-01 mission
    • M.C. Vaney, S. Maignan, M. Riès-Kautt, and A. Ducruix High-resolution structure (1.33 Å) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from spaceHab-01 mission Acta Crystallogr. D 52 1996 505 517
    • (1996) Acta Crystallogr. D , vol.52 , pp. 505-517
    • Vaney, M.C.1    Maignan, S.2    Riès-Kautt, M.3    Ducruix, A.4
  • 13
    • 0031791521 scopus 로고    scopus 로고
    • +â€"Try) interactions in the crystal structure of tetragonal lysozyme
    • +â€"Try) interactions in the crystal structure of tetragonal lysozyme Protein Sci. 7 1998 2472 2475
    • (1998) Protein Sci. , vol.7 , pp. 2472-2475
    • Wouters, J.1
  • 15
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • A.T. Brünger Crystallography & NMR system: a new software suite for macromolecular structure determination Acta Crystallogr. D 54 1998 905 921
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 17
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24 1991 946 950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 18
    • 49949136328 scopus 로고
    • Fluorescence and protein structure
    • R.W. Cowgill Fluorescence and protein structure Biochem. Biophys. Acta 140 1967 37 44
    • (1967) Biochem. Biophys. Acta , vol.140 , pp. 37-44
    • Cowgill, R.W.1
  • 19
    • 0015343130 scopus 로고
    • Fluorescence of lysozyme: Emission from tryptophan residues 62 and 108 and energy migration
    • T. Imoto, L.S. Forster, J.A. Rupley, and F. Tanaka Fluorescence of lysozyme: emission from tryptophan residues 62 and 108 and energy migration Proc. Natl. Acad. Sci. USA 69 1971 1151 1155
    • (1971) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 1151-1155
    • Imoto, T.1    Forster, L.S.2    Rupley, J.A.3    Tanaka, F.4
  • 20
    • 0024284778 scopus 로고
    • Characterization of individual tryptophan side chains in proteins using raman spectroscopy and hydrogenâ€"deuterium exchange kinetics
    • T. Miura, H. Takeuchi, and I. Harada Characterization of individual tryptophan side chains in proteins using raman spectroscopy and hydrogenâ€"deuterium exchange kinetics Biochemistry 27 1988 88 94
    • (1988) Biochemistry , vol.27 , pp. 88-94
    • Miura, T.1    Takeuchi, H.2    Harada, I.3
  • 21
    • 0025778735 scopus 로고
    • Lysozyme revisited: Crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D
    • N.C.J. Strynadka, and M.N.G. James Lysozyme revisited: crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D J. Mol. Biol. 220 1991 401 424
    • (1991) J. Mol. Biol. , vol.220 , pp. 401-424
    • Strynadka, N.C.J.1    James, M.N.G.2
  • 22
    • 0026551529 scopus 로고
    • Refinement of an enzyme complex with inhibitor bound at partial occupancy. Hen egg-white lysozyme and tri-N-acetylchitotriose at 1.75 a resolution
    • J.C. Cheetham, P.J. Artymiuk, and D.C. Phillips Refinement of an enzyme complex with inhibitor bound at partial occupancy. Hen egg-white lysozyme and tri-N-acetylchitotriose at 1.75 A resolution J. Mol. Biol. 224 1992 613 628
    • (1992) J. Mol. Biol. , vol.224 , pp. 613-628
    • Cheetham, J.C.1    Artymiuk, P.J.2    Phillips, D.C.3
  • 23
    • 0028932655 scopus 로고
    • Structures of partridge egg-white lysozyme with and without tri-N-acetylchitotriose inhibitor at 1.9 a resolution
    • M.A. Turner, and P.L. Howell Structures of partridge egg-white lysozyme with and without tri-N-acetylchitotriose inhibitor at 1.9 A resolution Protein Sci. 4 1995 442 449
    • (1995) Protein Sci. , vol.4 , pp. 442-449
    • Turner, M.A.1    Howell, P.L.2
  • 24
    • 0029328390 scopus 로고
    • The steady state and time-resolved fluorescence studies on the lysozymeâ€"ligand interaction
    • S. Yamashita, E. Nishimoto, and N. Yamazaki The steady state and time-resolved fluorescence studies on the lysozymeâ€"ligand interaction Biosci. Biotechnol. Biochem. (Tokyo) 59 1995 1255 1261
    • (1995) Biosci. Biotechnol. Biochem. (Tokyo) , vol.59 , pp. 1255-1261
    • Yamashita, S.1    Nishimoto, E.2    Yamazaki, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.