메뉴 건너뛰기




Volumn 1784, Issue 2, 2008, Pages 415-422

Detection of local polarity and conformational changes at the active site of rabbit muscle creatine kinase with a new arginine-specific fluorescent probe

Author keywords

Active site; Arginine specific labeling; Conformational changes; Fluorescent probes; Local polarity detection

Indexed keywords

ARGININE; CREATINE KINASE; FLUORESCENT DYE; PHENYLGLYOXAL;

EID: 38549102641     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.11.009     Document Type: Article
Times cited : (12)

References (59)
  • 1
    • 0000172594 scopus 로고
    • Use of "reporter groups" in structure-function studies of proteins
    • Burr M., and Koshland Jr. D.E. Use of "reporter groups" in structure-function studies of proteins. Proc. Natl. Acad. Sci. U. S. A 52 (1964) 1017-1024
    • (1964) Proc. Natl. Acad. Sci. U. S. A , vol.52 , pp. 1017-1024
    • Burr, M.1    Koshland Jr., D.E.2
  • 2
    • 0013913805 scopus 로고
    • Study of the polarity of the active site of chymotrypsin
    • Kallos J., and Avatis K. Study of the polarity of the active site of chymotrypsin. Biochemistry 5 (1966) 1979-1983
    • (1966) Biochemistry , vol.5 , pp. 1979-1983
    • Kallos, J.1    Avatis, K.2
  • 3
    • 0014196433 scopus 로고
    • The environment of a reporter group at the active site of chymotrypsin
    • Burr M.H., and Koshland Jr. D.E. The environment of a reporter group at the active site of chymotrypsin. J. Am. Chem. Soc 89 (1967) 5945-5951
    • (1967) J. Am. Chem. Soc , vol.89 , pp. 5945-5951
    • Burr, M.H.1    Koshland Jr., D.E.2
  • 4
    • 0014037680 scopus 로고
    • Environmentally sensitive tyrosyl residues. Nitration with tetranitromethane
    • Riordan J.F., Sokolovsky M., and Vallee B.L. Environmentally sensitive tyrosyl residues. Nitration with tetranitromethane. Biochemistry 6 (1967) 358-361
    • (1967) Biochemistry , vol.6 , pp. 358-361
    • Riordan, J.F.1    Sokolovsky, M.2    Vallee, B.L.3
  • 5
    • 8444226442 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, New York
    • Simpson R.J. Proteins and Proteomics (2003), Cold Spring Harbor Laboratory Press, New York
    • (2003) Proteins and Proteomics
    • Simpson, R.J.1
  • 6
    • 34250800262 scopus 로고    scopus 로고
    • Biochemical and functional characterization of UDP-galactose 4-epimerase from Aeromonas hydrophila
    • Agarwal S., Gopal K., Upadhyaya T., and Dixit A. Biochemical and functional characterization of UDP-galactose 4-epimerase from Aeromonas hydrophila. Biochim. Biophys. Acta 1774 (2007) 828-837
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 828-837
    • Agarwal, S.1    Gopal, K.2    Upadhyaya, T.3    Dixit, A.4
  • 7
    • 4244215808 scopus 로고    scopus 로고
    • Probing the caspase-3 active site by fluorescence lifetime measurements
    • Kyoung M., Kim S.Y., Seok H.Y., Park I.S., and Lee M. Probing the caspase-3 active site by fluorescence lifetime measurements. Biochim. Biophys. Acta 1598 (2002) 74-79
    • (2002) Biochim. Biophys. Acta , vol.1598 , pp. 74-79
    • Kyoung, M.1    Kim, S.Y.2    Seok, H.Y.3    Park, I.S.4    Lee, M.5
  • 8
    • 33947644330 scopus 로고    scopus 로고
    • Fluorescence spectroscopic analysis of the proximity changes between the central helix of troponin C and the C-terminus of troponin T from chicken skeletal muscle
    • Liou Y.M., and Chao H.L. Fluorescence spectroscopic analysis of the proximity changes between the central helix of troponin C and the C-terminus of troponin T from chicken skeletal muscle. Biochim. Biophys. Acta 1774 (2007) 466-473
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 466-473
    • Liou, Y.M.1    Chao, H.L.2
  • 9
    • 2442688260 scopus 로고    scopus 로고
    • Direct production of proteins with N-terminal cysteine for site-specific conjugation
    • Gentle I.E., Souza D.P.D., and Baca M. Direct production of proteins with N-terminal cysteine for site-specific conjugation. Bioconjug. Chem 15 (2004) 658-663
    • (2004) Bioconjug. Chem , vol.15 , pp. 658-663
    • Gentle, I.E.1    Souza, D.P.D.2    Baca, M.3
  • 10
    • 0037124666 scopus 로고    scopus 로고
    • New methods for proteomic research: Preparation of proteins with N-terminal cysteines for labeling and conjugation
    • Tolbert T.J., and Wong C.H. New methods for proteomic research: Preparation of proteins with N-terminal cysteines for labeling and conjugation. Angew. Chem., Int. Ed. 41 (2002) 2171-2174
    • (2002) Angew. Chem., Int. Ed. , vol.41 , pp. 2171-2174
    • Tolbert, T.J.1    Wong, C.H.2
  • 11
    • 0035797915 scopus 로고    scopus 로고
    • An unusually low pKa for Cys282 in the active site of human muscle creatine kinase
    • Wang P.F., McLeish M.J., Kneen M.M., Lee G., and Kenyon G.L. An unusually low pKa for Cys282 in the active site of human muscle creatine kinase. Biochemistry 40 (2001) 11698-11705
    • (2001) Biochemistry , vol.40 , pp. 11698-11705
    • Wang, P.F.1    McLeish, M.J.2    Kneen, M.M.3    Lee, G.4    Kenyon, G.L.5
  • 12
    • 0642337734 scopus 로고    scopus 로고
    • Effects of arginine on rabbit muscle creatine kinase and salt-induced molten globule-like state
    • Ou W.B., Wang R.S., Lu J., and Zhou H.M. Effects of arginine on rabbit muscle creatine kinase and salt-induced molten globule-like state. Biochim. Biophys. Acta 1652 (2003) 7-16
    • (2003) Biochim. Biophys. Acta , vol.1652 , pp. 7-16
    • Ou, W.B.1    Wang, R.S.2    Lu, J.3    Zhou, H.M.4
  • 13
    • 0017365503 scopus 로고
    • Arginyl residues: anion recognition sites in enzymes
    • Riordan J.F., McElvany K.D., and Borders Jr. C.L. Arginyl residues: anion recognition sites in enzymes. Science 195 (1977) 884-886
    • (1977) Science , vol.195 , pp. 884-886
    • Riordan, J.F.1    McElvany, K.D.2    Borders Jr., C.L.3
  • 14
    • 0016717899 scopus 로고
    • An essential arginyl residue at the nucleotide binding site of creatine kinase
    • Borders Jr. C.L., and Riordan J.F. An essential arginyl residue at the nucleotide binding site of creatine kinase. Biochemistry 14 (1975) 4699-4704
    • (1975) Biochemistry , vol.14 , pp. 4699-4704
    • Borders Jr., C.L.1    Riordan, J.F.2
  • 15
    • 0032584106 scopus 로고    scopus 로고
    • Creatine kinase: Essential arginine residues at the nucleotide binding site identified by chemical modification and high-resolution tandem mass spectrometry
    • Wood T.D., Guan Z.Q., Borders Jr. C.L., Chen L.H., Kenyon G.L., and McLafferty F.W. Creatine kinase: Essential arginine residues at the nucleotide binding site identified by chemical modification and high-resolution tandem mass spectrometry. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 3362-3365
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 3362-3365
    • Wood, T.D.1    Guan, Z.Q.2    Borders Jr., C.L.3    Chen, L.H.4    Kenyon, G.L.5    McLafferty, F.W.6
  • 16
    • 33745389201 scopus 로고    scopus 로고
    • Impact of intra-subunit domain-domain interactions on creatine kinase activity and stability
    • Zhao T.J., Feng S., Wang Y.L., Liu Y., Luo X.C., Zhou H.M., and Yan Y.B. Impact of intra-subunit domain-domain interactions on creatine kinase activity and stability. FEBS Lett. 580 (2006) 3835-3840
    • (2006) FEBS Lett. , vol.580 , pp. 3835-3840
    • Zhao, T.J.1    Feng, S.2    Wang, Y.L.3    Liu, Y.4    Luo, X.C.5    Zhou, H.M.6    Yan, Y.B.7
  • 18
    • 0024497567 scopus 로고
    • Creatine kinase isoforms in ischemic heart disease
    • Wu A.H. Creatine kinase isoforms in ischemic heart disease. Clin. Chem. 35 (1989) 7-13
    • (1989) Clin. Chem. , vol.35 , pp. 7-13
    • Wu, A.H.1
  • 19
    • 0023137068 scopus 로고
    • Carrier detection in Duchenne muscular dystrophy: A review of current issues and approaches
    • Gruemer H.D., and Prior T. Carrier detection in Duchenne muscular dystrophy: A review of current issues and approaches. Clin. Chim. Acta 162 (1987) 1-18
    • (1987) Clin. Chim. Acta , vol.162 , pp. 1-18
    • Gruemer, H.D.1    Prior, T.2
  • 21
    • 0032515099 scopus 로고    scopus 로고
    • Crystal structure of rabbit muscle creatine kinase
    • Rao J.K.M., Bujacz G., and Wlodawer A. Crystal structure of rabbit muscle creatine kinase. FEBS Lett. 439 (1998) 133-137
    • (1998) FEBS Lett. , vol.439 , pp. 133-137
    • Rao, J.K.M.1    Bujacz, G.2    Wlodawer, A.3
  • 26
    • 0016651874 scopus 로고
    • Reversible modification of arginine residues
    • Patthy L., and Smith E.L. Reversible modification of arginine residues. J. Biol. Chem. 250 (1975) 557-564
    • (1975) J. Biol. Chem. , vol.250 , pp. 557-564
    • Patthy, L.1    Smith, E.L.2
  • 27
    • 0014410251 scopus 로고
    • The reaction of phenylglyoxal with arginine residues in proteins
    • Takahashi K. The reaction of phenylglyoxal with arginine residues in proteins. J. Biol. Chem 243 (1968) 6171-6179
    • (1968) J. Biol. Chem , vol.243 , pp. 6171-6179
    • Takahashi, K.1
  • 28
    • 0019276655 scopus 로고
    • Modification of available arginine residues in proteins by p-hydroxyphenylglyoxal
    • Yamasaki R.B., Vega A., and Feeney R.E. Modification of available arginine residues in proteins by p-hydroxyphenylglyoxal. Anal. Biochem. 109 (1980) 32-40
    • (1980) Anal. Biochem. , vol.109 , pp. 32-40
    • Yamasaki, R.B.1    Vega, A.2    Feeney, R.E.3
  • 29
    • 0019547083 scopus 로고
    • Colorimetric determination of arginine residues in proteins by p-nitrophenylglyoxal
    • Yamasaki R.B., Shimer D.A., and Feeney R.E. Colorimetric determination of arginine residues in proteins by p-nitrophenylglyoxal. Anal. Biochem. 111 (1981) 220-226
    • (1981) Anal. Biochem. , vol.111 , pp. 220-226
    • Yamasaki, R.B.1    Shimer, D.A.2    Feeney, R.E.3
  • 31
    • 0019877627 scopus 로고
    • p-Azidophenylglyoxal A heterobifunctional photoactivable cross-linking reagent selective for arginyl residues
    • Ngo T.T., Yam C.F., Lenhoff H.M., and Ivy J. p-Azidophenylglyoxal A heterobifunctional photoactivable cross-linking reagent selective for arginyl residues. J. Biol. Chem. 256 (1981) 11313-11318
    • (1981) J. Biol. Chem. , vol.256 , pp. 11313-11318
    • Ngo, T.T.1    Yam, C.F.2    Lenhoff, H.M.3    Ivy, J.4
  • 32
    • 0015909395 scopus 로고
    • Functional arginyl residues in carboxypeptidase A. Modification with butanedione
    • Riordan J.F. Functional arginyl residues in carboxypeptidase A. Modification with butanedione. Biochemistry 12 (1973) 3915-3923
    • (1973) Biochemistry , vol.12 , pp. 3915-3923
    • Riordan, J.F.1
  • 33
    • 0018801592 scopus 로고
    • Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase
    • Malinowski D.P., and Fridovich I. Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase. Biochemistry 18 (1979) 5909-5917
    • (1979) Biochemistry , vol.18 , pp. 5909-5917
    • Malinowski, D.P.1    Fridovich, I.2
  • 35
    • 0019000195 scopus 로고
    • Origin of the selectivity of α-dicarbonyl reagents for arginyl residues of anion-binding sites
    • Patthy L., and Thész J. Origin of the selectivity of α-dicarbonyl reagents for arginyl residues of anion-binding sites. Eur. J. Biochem. 105 (1980) 387-393
    • (1980) Eur. J. Biochem. , vol.105 , pp. 387-393
    • Patthy, L.1    Thész, J.2
  • 36
    • 0028218043 scopus 로고
    • HOCGO and DMACGO. Two coumarin derived α-dicarbonyls suitable as pH and polarity sensitive fluorescent reporters for proteins that can be targeted at reactive arginines
    • Baburaj K., Azam N., Udgaonkar D., and Durani S. HOCGO and DMACGO. Two coumarin derived α-dicarbonyls suitable as pH and polarity sensitive fluorescent reporters for proteins that can be targeted at reactive arginines. Biochim. Biophys. Acta 1199 (1994) 253-265
    • (1994) Biochim. Biophys. Acta , vol.1199 , pp. 253-265
    • Baburaj, K.1    Azam, N.2    Udgaonkar, D.3    Durani, S.4
  • 39
    • 0034663548 scopus 로고    scopus 로고
    • Neutral red as a hydrophobic probe for monitoring neuronal activity
    • Okada D. Neutral red as a hydrophobic probe for monitoring neuronal activity. J. Neurosci. Methods 101 (2000) 85-92
    • (2000) J. Neurosci. Methods , vol.101 , pp. 85-92
    • Okada, D.1
  • 40
    • 14844358216 scopus 로고    scopus 로고
    • Detection of local polarity of α-lactalbumin by N-terminal specific labeling with a new tailor-made fluorescent probe
    • Dong S.Y., Ma H.M., Duan X.J., Chen X.Q., and Li J. Detection of local polarity of α-lactalbumin by N-terminal specific labeling with a new tailor-made fluorescent probe. J. Proteome Res. 4 (2005) 161-166
    • (2005) J. Proteome Res. , vol.4 , pp. 161-166
    • Dong, S.Y.1    Ma, H.M.2    Duan, X.J.3    Chen, X.Q.4    Li, J.5
  • 41
    • 30744474722 scopus 로고    scopus 로고
    • Characterization of local polarity and hydrophobic binding sites of β-lactoglobulin by using N-terminal specific fluorescence labeling
    • Dong S.Y., Zhao Z.W., and Ma H.M. Characterization of local polarity and hydrophobic binding sites of β-lactoglobulin by using N-terminal specific fluorescence labeling. J. Proteome Res. 5 (2006) 26-31
    • (2006) J. Proteome Res. , vol.5 , pp. 26-31
    • Dong, S.Y.1    Zhao, Z.W.2    Ma, H.M.3
  • 42
    • 27644508338 scopus 로고    scopus 로고
    • Local dynamics measured by hydrogen/deuterium exchange and mass spectrometry of creatine kinase digested by two proteases
    • Mazon H., Marcillat O., Forest E., and Vial C. Local dynamics measured by hydrogen/deuterium exchange and mass spectrometry of creatine kinase digested by two proteases. Biochimie 87 (2005) 1101-1110
    • (2005) Biochimie , vol.87 , pp. 1101-1110
    • Mazon, H.1    Marcillat, O.2    Forest, E.3    Vial, C.4
  • 43
    • 0037177517 scopus 로고    scopus 로고
    • New triazine spectroscopic reagent for the separation of DL-amino acids by micellar electrokinetic chromatography
    • Ma H.M., Wang Z.H., and Su M.H. New triazine spectroscopic reagent for the separation of DL-amino acids by micellar electrokinetic chromatography. J. Chromatogr. A 955 (2002) 125-131
    • (2002) J. Chromatogr. A , vol.955 , pp. 125-131
    • Ma, H.M.1    Wang, Z.H.2    Su, M.H.3
  • 44
    • 0001496514 scopus 로고
    • A synthesis of adrenaline-like compounds
    • Fodor G., and Kovács Ö. A synthesis of adrenaline-like compounds. J. Am. Chem. Soc. 71 (1949) 1045-1048
    • (1949) J. Am. Chem. Soc. , vol.71 , pp. 1045-1048
    • Fodor, G.1    Kovács, Ö.2
  • 45
    • 1842543819 scopus 로고
    • New antiviral compounds with considerable activity in vivo. IV. Aromatic α-keto aldehydes
    • Cavallini G. New antiviral compounds with considerable activity in vivo. IV. Aromatic α-keto aldehydes. J. Med. Chem. 7 (1964) 255-258
    • (1964) J. Med. Chem. , vol.7 , pp. 255-258
    • Cavallini, G.1
  • 46
    • 0842330741 scopus 로고    scopus 로고
    • Pyridinium-carbaldehyde: active Maillard reaction product from the reaction of hexoses with lysine residues
    • Reihl O., Biemel K.M., Lederer M.O., and Schwack W. Pyridinium-carbaldehyde: active Maillard reaction product from the reaction of hexoses with lysine residues. Carbohydr. Res. 339 (2004) 705-714
    • (2004) Carbohydr. Res. , vol.339 , pp. 705-714
    • Reihl, O.1    Biemel, K.M.2    Lederer, M.O.3    Schwack, W.4
  • 47
    • 0027502655 scopus 로고
    • Conformational changes at the active site of creatine kinase at low concentrations of guanidinium chloride
    • Zhou H.M., Zhang X.H., Yin Y., and Tsou C.L. Conformational changes at the active site of creatine kinase at low concentrations of guanidinium chloride. Biochem. J. 291 (1993) 103-107
    • (1993) Biochem. J. , vol.291 , pp. 103-107
    • Zhou, H.M.1    Zhang, X.H.2    Yin, Y.3    Tsou, C.L.4
  • 48
    • 0029339299 scopus 로고
    • Subcellular localization of and photosensitization by protoporphyrin IX in human keratinocytes and fibroblasts cultivated with 5-aminolevulinic acid
    • Gaullier J.M., Gèze M., Santus R., Melo T.S., Mazière J.C., Bazin M., Molière P., and Dubertret L. Subcellular localization of and photosensitization by protoporphyrin IX in human keratinocytes and fibroblasts cultivated with 5-aminolevulinic acid. Photochem. Photobiol. 62 (1995) 114-122
    • (1995) Photochem. Photobiol. , vol.62 , pp. 114-122
    • Gaullier, J.M.1    Gèze, M.2    Santus, R.3    Melo, T.S.4    Mazière, J.C.5    Bazin, M.6    Molière, P.7    Dubertret, L.8
  • 49
    • 0028047699 scopus 로고
    • Extent and rate of proton release by photosynthetic water oxidation in thylakoids: Electrostatic relaxation versus chemical production
    • Haumann M., and Junge W. Extent and rate of proton release by photosynthetic water oxidation in thylakoids: Electrostatic relaxation versus chemical production. Biochemistry 33 (1994) 864-872
    • (1994) Biochemistry , vol.33 , pp. 864-872
    • Haumann, M.1    Junge, W.2
  • 50
    • 4043138930 scopus 로고    scopus 로고
    • Recognition of guanine by a designed triazine-based fluorescent probe through intermolecular multiple hydrogen bonding
    • Ma H.M., Nie L.H., and Xiong S.X. Recognition of guanine by a designed triazine-based fluorescent probe through intermolecular multiple hydrogen bonding. Supramol. Chem. 16 (2004) 311-317
    • (2004) Supramol. Chem. , vol.16 , pp. 311-317
    • Ma, H.M.1    Nie, L.H.2    Xiong, S.X.3
  • 52
    • 0015750297 scopus 로고
    • Structural properties of the creatine-kinase active site studied by chromophoric-reagent labelling
    • Roustan C., Brevet A., and Pradel L.A. Structural properties of the creatine-kinase active site studied by chromophoric-reagent labelling. Eur. J. Biochem. 39 (1973) 371-379
    • (1973) Eur. J. Biochem. , vol.39 , pp. 371-379
    • Roustan, C.1    Brevet, A.2    Pradel, L.A.3
  • 53
    • 0031715149 scopus 로고    scopus 로고
    • Inactivation of creatine kinase is due to the conformational changes of the active sites during thermal denaturation
    • Bai J.H., Zheng S.Y., and Zhou H.M. Inactivation of creatine kinase is due to the conformational changes of the active sites during thermal denaturation. Biochem. Mol. Biol. Int. 45 (1998) 941-951
    • (1998) Biochem. Mol. Biol. Int. , vol.45 , pp. 941-951
    • Bai, J.H.1    Zheng, S.Y.2    Zhou, H.M.3
  • 55
    • 0028847259 scopus 로고
    • Effects of pH and KCl on the conformations of creatine kinase from rabbit muscle. Infrared, circular dichroic and fluorescence studies
    • Raimbault C., Couthon F., Vial C., and Buchet R. Effects of pH and KCl on the conformations of creatine kinase from rabbit muscle. Infrared, circular dichroic and fluorescence studies. Eur. J. Biochem. 234 (1995) 570-578
    • (1995) Eur. J. Biochem. , vol.234 , pp. 570-578
    • Raimbault, C.1    Couthon, F.2    Vial, C.3    Buchet, R.4
  • 57
    • 0021755632 scopus 로고
    • Comparison of the rates of inactivation and conformational changes of creatine kinase during urea denaturation
    • Yao Q.Z., Tian M., and Tsou C.L. Comparison of the rates of inactivation and conformational changes of creatine kinase during urea denaturation. Biochemistry 23 (1984) 2740-2744
    • (1984) Biochemistry , vol.23 , pp. 2740-2744
    • Yao, Q.Z.1    Tian, M.2    Tsou, C.L.3
  • 58
    • 0028866093 scopus 로고
    • Spin-labeling probe on conformational change at the active sites of creatine kinase during denaturation by guanidine hydrochloride
    • Liu Z.J., and Zhou J.M. Spin-labeling probe on conformational change at the active sites of creatine kinase during denaturation by guanidine hydrochloride. Biochim. Biophys. Acta 1253 (1995) 63-68
    • (1995) Biochim. Biophys. Acta , vol.1253 , pp. 63-68
    • Liu, Z.J.1    Zhou, J.M.2
  • 59
    • 0001216718 scopus 로고
    • Location of the active sites of some enzymes in limited and flexible molecular regions
    • Tsou C.L. Location of the active sites of some enzymes in limited and flexible molecular regions. Trends Biochem. Sci. 11 (1986) 427-429
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 427-429
    • Tsou, C.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.