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Volumn 92, Issue 4, 2007, Pages 1192-1203

Structural stabilization and functional improvement of horseradish peroxidase upon modification of accessible lysines: Experiments and simulation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANTHRAQUINONE 2 CARBOXYLIC ACID; AROMATIC COMPOUND; CARBOXYLIC ACID DERIVATIVE; HORSERADISH PEROXIDASE; HYDROGEN PEROXIDE; LYSINE; OXIDOREDUCTASE; PEROXIDE; UNCLASSIFIED DRUG;

EID: 33846833785     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.092858     Document Type: Article
Times cited : (84)

References (68)
  • 1
    • 0002154654 scopus 로고
    • Horseradish peroxidases: Structure and kinetic properties
    • I. K. E. Everse and M. B. Grisham, editors. CRC Press/Boca Raton, FL
    • Dunford, H. B. 1991. Horseradish peroxidases: structure and kinetic properties. In Peroxidases in Chemistry and Biology. I. K. E. Everse and M. B. Grisham, editors. CRC Press/Boca Raton, FL. 1-24.
    • (1991) Peroxidases in Chemistry and Biology , pp. 1-24
    • Dunford, H.B.1
  • 2
    • 0742324902 scopus 로고    scopus 로고
    • Horseradish peroxidase: A modern view of a classic enzyme
    • Nigel, C. V. 2004. Horseradish peroxidase: a modern view of a classic enzyme. Phytochemistry. 65:249-259.
    • (2004) Phytochemistry , vol.65 , pp. 249-259
    • Nigel, C.V.1
  • 4
    • 0022427616 scopus 로고
    • Plant peroxidases. Their primary, secondary and tertiary structures and relation to cytochrome c peroxidase
    • Welinder, K. G. 1985. Plant peroxidases. Their primary, secondary and tertiary structures and relation to cytochrome c peroxidase. Eur. J. Biochem. 151:497-504.
    • (1985) Eur. J. Biochem , vol.151 , pp. 497-504
    • Welinder, K.G.1
  • 5
    • 0018488111 scopus 로고
    • Amino acid sequence studies of horseradish peroxidase
    • Welinder, K. G. 1979. Amino acid sequence studies of horseradish peroxidase. Eur. J. Biochem. 95:483-502.
    • (1979) Eur. J. Biochem , vol.95 , pp. 483-502
    • Welinder, K.G.1
  • 7
    • 0017041348 scopus 로고
    • Covalent structure of the glycoprotein horseradish peroxidase
    • Welinder, K. G. 1976. Covalent structure of the glycoprotein horseradish peroxidase. FEBS Lett. 72:19-23.
    • (1976) FEBS Lett , vol.72 , pp. 19-23
    • Welinder, K.G.1
  • 8
    • 0017251905 scopus 로고
    • The isolation and characterization of the glycopeptides from horseradish peroxidase isoenzymes C
    • Clarke, J., and L. M. Shannon. 1976. The isolation and characterization of the glycopeptides from horseradish peroxidase isoenzymes C. Biochim. Biophys. Acta. 421:428-442.
    • (1976) Biochim. Biophys. Acta , vol.421 , pp. 428-442
    • Clarke, J.1    Shannon, L.M.2
  • 9
    • 0030596471 scopus 로고    scopus 로고
    • The glycans of horseradish peroxidase
    • Yang, B. Y., J. S. S. Gray, and R. Montgomery. 1996. The glycans of horseradish peroxidase. Carbohydr. Res. 287:203-212.
    • (1996) Carbohydr. Res , vol.287 , pp. 203-212
    • Yang, B.Y.1    Gray, J.S.S.2    Montgomery, R.3
  • 12
    • 0032474438 scopus 로고    scopus 로고
    • Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by x-ray crystallography
    • Henriksen, A., D. J. Schuller, K. Meno, K. G. Welinder, A. T. Smith, and M. Gajhede. 1998. Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by x-ray crystallography. Biochemistry. 37:8054-8060.
    • (1998) Biochemistry , vol.37 , pp. 8054-8060
    • Henriksen, A.1    Schuller, D.J.2    Meno, K.3    Welinder, K.G.4    Smith, A.T.5    Gajhede, M.6
  • 13
    • 0034639435 scopus 로고    scopus 로고
    • Filizola, M., and G. H. Loew. 2000. Role of protein environment in horseradish peroxidase compound I formation: molecular dynamics simulations of horseradish peroxidase-HOOH complex. J. Am. Chem. Soc. 122:18-25.
    • Filizola, M., and G. H. Loew. 2000. Role of protein environment in horseradish peroxidase compound I formation: molecular dynamics simulations of horseradish peroxidase-HOOH complex. J. Am. Chem. Soc. 122:18-25.
  • 14
    • 0033521007 scopus 로고    scopus 로고
    • The structures of the horseradish peroxidase C-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates
    • Henriksen, A., A. T. Smith, and M. Gajhede. 1999. The structures of the horseradish peroxidase C-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates. J. Biol. Chem. 274:35005-35011.
    • (1999) J. Biol. Chem , vol.274 , pp. 35005-35011
    • Henriksen, A.1    Smith, A.T.2    Gajhede, M.3
  • 15
    • 12144267622 scopus 로고    scopus 로고
    • Complexes of horseradish peroxidase with formate, acetate, and carbon monoxide
    • Carlsson, G. H., P. Nicholls, D. Svistunenko, G. I. Berglund, and J. Hajdu. 2005. Complexes of horseradish peroxidase with formate, acetate, and carbon monoxide. Biochemistry. 44:635-642.
    • (2005) Biochemistry , vol.44 , pp. 635-642
    • Carlsson, G.H.1    Nicholls, P.2    Svistunenko, D.3    Berglund, G.I.4    Hajdu, J.5
  • 16
    • 0035822698 scopus 로고    scopus 로고
    • Aromatic substrate specificity of horseradish peroxidase C studied by a combined fluorescence line narrowing/energy minimization approach: The effect of localized side-chain reorganization
    • Laberge, M., S. Osvath, and J. Fidy. 2001. Aromatic substrate specificity of horseradish peroxidase C studied by a combined fluorescence line narrowing/energy minimization approach: the effect of localized side-chain reorganization. Biochemistry. 40:9226-9237.
    • (2001) Biochemistry , vol.40 , pp. 9226-9237
    • Laberge, M.1    Osvath, S.2    Fidy, J.3
  • 17
    • 16344387923 scopus 로고    scopus 로고
    • Heme peroxidase clothing and inhibition with polyphenolic substances revealed by molecular modeling
    • Ziemys, A., and J. Kulys. 2005. Heme peroxidase clothing and inhibition with polyphenolic substances revealed by molecular modeling. Comput. Biol. Chem. 29:83-90.
    • (2005) Comput. Biol. Chem , vol.29 , pp. 83-90
    • Ziemys, A.1    Kulys, J.2
  • 19
    • 0141739441 scopus 로고    scopus 로고
    • Solvent dependent and independent motions of CO-horseradish peroxidase examined by infrared spectroscopy and molecular dynamics calculations
    • Kaposi, A. D., N. V. Prabhu, S. D. Dalosto, K. A. Sharp, W. W. Wright, S. S. Stavrov, and J. M. Vanderkooi. 2003. Solvent dependent and independent motions of CO-horseradish peroxidase examined by infrared spectroscopy and molecular dynamics calculations. Biophys. Chem. 106:1-14.
    • (2003) Biophys. Chem , vol.106 , pp. 1-14
    • Kaposi, A.D.1    Prabhu, N.V.2    Dalosto, S.D.3    Sharp, K.A.4    Wright, W.W.5    Stavrov, S.S.6    Vanderkooi, J.M.7
  • 20
    • 0035798657 scopus 로고    scopus 로고
    • The critical role of the proximal calcium ion in the structural properties of horseradish peroxidase
    • Howes, B. D., A. Feis, L. Raimondi, C. Indiani, and G. Smulevich. 2001. The critical role of the proximal calcium ion in the structural properties of horseradish peroxidase. J. Biol. Chem. 276:40704-40711.
    • (2001) J. Biol. Chem , vol.276 , pp. 40704-40711
    • Howes, B.D.1    Feis, A.2    Raimondi, L.3    Indiani, C.4    Smulevich, G.5
  • 21
    • 0037379807 scopus 로고    scopus 로고
    • The endogenous calcium ions of horseradish peroxidase C are required to maintain the functional nonplanarity of the heme
    • Laberge, M., Q. Huang, R. Schweitzer-Stenner, and J. Fidy. 2003. The endogenous calcium ions of horseradish peroxidase C are required to maintain the functional nonplanarity of the heme. Biophys. J. 84:2542-2552.
    • (2003) Biophys. J , vol.84 , pp. 2542-2552
    • Laberge, M.1    Huang, Q.2    Schweitzer-Stenner, R.3    Fidy, J.4
  • 22
    • 0029151614 scopus 로고
    • Horseradish peroxidase His42Ala, His42Val, and Phe41Ala mutants: Histidine catalysis and control of substrate access to the heme iron
    • Newmyer, S. L., and P. R. Ortiz de Montellano. 1995. Horseradish peroxidase His42Ala, His42Val, and Phe41Ala mutants: histidine catalysis and control of substrate access to the heme iron. J. Biol. Chem. 270:19430-19438.
    • (1995) J. Biol. Chem , vol.270 , pp. 19430-19438
    • Newmyer, S.L.1    Ortiz de Montellano, P.R.2
  • 23
    • 0030068091 scopus 로고    scopus 로고
    • Role of arginine 38 in horseradish peroxidase: A critical residue for substrate binding and catalysis
    • Rodriguez-Lopez, J. N., A. T. Smith, and R. N. F. Thorneley. 1996. Role of arginine 38 in horseradish peroxidase: a critical residue for substrate binding and catalysis. J. Biol. Chem. 271:4023-4030.
    • (1996) J. Biol. Chem , vol.271 , pp. 4023-4030
    • Rodriguez-Lopez, J.N.1    Smith, A.T.2    Thorneley, R.N.F.3
  • 24
    • 0023644531 scopus 로고
    • Protein control of prosthetic heme reactivity. Reaction of substrates with the heme edge of horseradish peroxidase
    • Ator, M., and P. R. Ortiz de Montellano. 1987. Protein control of prosthetic heme reactivity. Reaction of substrates with the heme edge of horseradish peroxidase. J. Biol. Chem. 262:1542-1551.
    • (1987) J. Biol. Chem , vol.262 , pp. 1542-1551
    • Ator, M.1    Ortiz de Montellano, P.R.2
  • 26
    • 0031123383 scopus 로고    scopus 로고
    • Activity and stability of native and modified alanine aminotransferase in cosolvent systems and denaturants
    • Moreno, J. M., and C. Ó. Fágáin. 1997. Activity and stability of native and modified alanine aminotransferase in cosolvent systems and denaturants. J. Mol. Catal. B Enzym. 2:271-279.
    • (1997) J. Mol. Catal. B Enzym , vol.2 , pp. 271-279
    • Moreno, J.M.1    Fágáin, C.O.2
  • 28
    • 2642709180 scopus 로고    scopus 로고
    • Chemically stabilized trypsin used in dipeptide synthesis
    • Murphy, A., and C. Ó. Fágáin. 1998. Chemically stabilized trypsin used in dipeptide synthesis. Biotechnol. Bioeng. 58:366-373.
    • (1998) Biotechnol. Bioeng , vol.58 , pp. 366-373
    • Murphy, A.1    Fágáin, C.O.2
  • 30
    • 0018788891 scopus 로고
    • Chemical modification of the ε-amino groups of lysine residues in horseradish peroxidase and its effect on the catalytic properties and thermostability of the enzyme
    • Ugarova, N. N., G. D. Rozhkova, and I. V. Berezin. 1979. Chemical modification of the ε-amino groups of lysine residues in horseradish peroxidase and its effect on the catalytic properties and thermostability of the enzyme. Biochim. Biophys. Acta. 570:31-42.
    • (1979) Biochim. Biophys. Acta , vol.570 , pp. 31-42
    • Ugarova, N.N.1    Rozhkova, G.D.2    Berezin, I.V.3
  • 31
    • 0028363563 scopus 로고
    • Thermostabilized chemical derivatives of horseradish peroxidase
    • Ryan, O., M. R. Smyth, and C. Ó. Fágáin. 1994. Thermostabilized chemical derivatives of horseradish peroxidase. Enzyme Microb. Technol. 16:501-505.
    • (1994) Enzyme Microb. Technol , vol.16 , pp. 501-505
    • Ryan, O.1    Smyth, M.R.2    Fágáin, C.O.3
  • 32
    • 0030248390 scopus 로고    scopus 로고
    • Modification of horseradish peroxidase with bifunctional N- hydroxysuccinimide esters: Effects on molecular stability
    • Miland, E., M. R. Smyth, and C. Ó. Fágáin. 1996. Modification of horseradish peroxidase with bifunctional N- hydroxysuccinimide esters: effects on molecular stability. Enzyme Microb. Technol. 19:242-249.
    • (1996) Enzyme Microb. Technol , vol.19 , pp. 242-249
    • Miland, E.1    Smyth, M.R.2    Fágáin, C.O.3
  • 33
    • 0030444236 scopus 로고    scopus 로고
    • Chemical stabilization of recombinant horseradish peroxidase
    • O'Brien, A. M., and C. Ó. Fágáin. 1996. Chemical stabilization of recombinant horseradish peroxidase. Biotechnol. Tech. 10:905-910.
    • (1996) Biotechnol. Tech , vol.10 , pp. 905-910
    • O'Brien, A.M.1    Fágáin, C.O.2
  • 34
    • 0030200465 scopus 로고    scopus 로고
    • Increased thermal and solvent tolerance of acetylated horseradish peroxidase
    • Miland, E., M. R. Smyth, and C. Ó. Fágáin. 1996. Increased thermal and solvent tolerance of acetylated horseradish peroxidase. Enzyme Microb. Technol. 19:63-67.
    • (1996) Enzyme Microb. Technol , vol.19 , pp. 63-67
    • Miland, E.1    Smyth, M.R.2    Fágáin, C.O.3
  • 36
    • 0031984007 scopus 로고    scopus 로고
    • Kinetics of thermal inactivation of horseradish peroxidase: Stabilizing effect of methoxypoly(ethylene glycol)
    • Garcia, D., F. Ortéga, and J. L. Marty. 1998. Kinetics of thermal inactivation of horseradish peroxidase: stabilizing effect of methoxypoly(ethylene glycol). Biotechnol. Appl. Biochem. 27:49-54.
    • (1998) Biotechnol. Appl. Biochem , vol.27 , pp. 49-54
    • Garcia, D.1    Ortéga, F.2    Marty, J.L.3
  • 37
    • 0035829832 scopus 로고    scopus 로고
    • Location of crosslinks in chemically stabilized horseradish peroxidase. Implications for design of crosslinks
    • O'Brien, A. M., C. Ó. Fágáin, P. F. Nielsen, and K. G. Welinder. 2001. Location of crosslinks in chemically stabilized horseradish peroxidase. Implications for design of crosslinks. Biotechnol. Bioeng. 76:277-284.
    • (2001) Biotechnol. Bioeng , vol.76 , pp. 277-284
    • O'Brien, A.M.1    Fágáin, C.O.2    Nielsen, P.F.3    Welinder, K.G.4
  • 38
    • 0347297131 scopus 로고    scopus 로고
    • Effects of phthalic anhydride modification on horseradish peroxidase stability and activity
    • O'Brien, A. M., A. T. Smith, and C. Ó. Fágáin. 2003. Effects of phthalic anhydride modification on horseradish peroxidase stability and activity. Biotechnol. Bioeng. 81:233-240.
    • (2003) Biotechnol. Bioeng , vol.81 , pp. 233-240
    • O'Brien, A.M.1    Smith, A.T.2    Fágáin, C.O.3
  • 39
    • 0037375304 scopus 로고    scopus 로고
    • Treatment of aqueous chlorophenol by phthalic anhydride-modified horseradish peroxidase
    • Song, H. Y., J. Z. Liu, Y. H. Xiong, L. P. Weng, and L. N. Ji. 2003. Treatment of aqueous chlorophenol by phthalic anhydride-modified horseradish peroxidase. J. Mol. Catal. B Enzym. 22:37-44.
    • (2003) J. Mol. Catal. B Enzym , vol.22 , pp. 37-44
    • Song, H.Y.1    Liu, J.Z.2    Xiong, Y.H.3    Weng, L.P.4    Ji, L.N.5
  • 40
    • 27844536480 scopus 로고    scopus 로고
    • Horseradish peroxidase thermostabilization: The combinatorial effects of the surface modification and the polyols
    • Hassani, L., B. Ranjbar, K. Khajeh, H. Naderi-Manesh, M. Naderi-Manesh, and M. Sadeghi. 2006. Horseradish peroxidase thermostabilization: the combinatorial effects of the surface modification and the polyols. Enzyme Microb. Technol. 38:118-125.
    • (2006) Enzyme Microb. Technol , vol.38 , pp. 118-125
    • Hassani, L.1    Ranjbar, B.2    Khajeh, K.3    Naderi-Manesh, H.4    Naderi-Manesh, M.5    Sadeghi, M.6
  • 41
    • 33644891075 scopus 로고    scopus 로고
    • Increased thermal and organic solvent tolerance of modified horseradish peroxidase
    • Liu, J. Z., T. L. Wang, M. T. Huang, H. Y. Song, L. P. Weng, and L. N. Ji. 2006. Increased thermal and organic solvent tolerance of modified horseradish peroxidase. Protein Eng. Des. Sel. 19:169-173.
    • (2006) Protein Eng. Des. Sel , vol.19 , pp. 169-173
    • Liu, J.Z.1    Wang, T.L.2    Huang, M.T.3    Song, H.Y.4    Weng, L.P.5    Ji, L.N.6
  • 42
    • 0026078438 scopus 로고
    • Use of pyrocarbonates for chemical modification of histidine residues of horseradish peroxidase
    • Urrutigoity, M., M. Baboulene, and A. Lattes. 1991. Use of pyrocarbonates for chemical modification of histidine residues of horseradish peroxidase. Bioorg. Chem. 19:66-76.
    • (1991) Bioorg. Chem , vol.19 , pp. 66-76
    • Urrutigoity, M.1    Baboulene, M.2    Lattes, A.3
  • 43
    • 11844291287 scopus 로고    scopus 로고
    • Manipulating proteins with chemistry: A cross-section of chemical biology
    • Hahn, M. E., and T. W. Muir. 2005. Manipulating proteins with chemistry: a cross-section of chemical biology. Trends Biochem. Sci. 30:26-34.
    • (2005) Trends Biochem. Sci , vol.30 , pp. 26-34
    • Hahn, M.E.1    Muir, T.W.2
  • 44
    • 17044418114 scopus 로고    scopus 로고
    • Anthraquinone 2-carboxylic acid as an electron shuttling mediator and attached electron relay for horseradish peroxidase
    • Mogharrab, N., and H. Ghourchian. 2005. Anthraquinone 2-carboxylic acid as an electron shuttling mediator and attached electron relay for horseradish peroxidase. Electrochem. Commun. 7:466-471.
    • (2005) Electrochem. Commun , vol.7 , pp. 466-471
    • Mogharrab, N.1    Ghourchian, H.2
  • 45
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 46
    • 0013889689 scopus 로고
    • Determination of free amino groups in proteins by trinitrobenzenesulfonic acid
    • Habeeb, A. S. F. A. 1966. Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. Anal. Biochem. 14:328-336.
    • (1966) Anal. Biochem , vol.14 , pp. 328-336
    • Habeeb, A.S.F.A.1
  • 47
    • 0026614994 scopus 로고
    • The determination of ε-amino groups in soluble and poorly soluble proteinaceous materials by a spectrophotometric method using trinitrobenzenesulfonic acid
    • Bubnis, W., and C. Ofner. 1992. The determination of ε-amino groups in soluble and poorly soluble proteinaceous materials by a spectrophotometric method using trinitrobenzenesulfonic acid. Anal. Biochem. 297:129-133.
    • (1992) Anal. Biochem , vol.297 , pp. 129-133
    • Bubnis, W.1    Ofner, C.2
  • 49
    • 0034736285 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Revisiting the thermodynamic parameters of activation may explain local flexibility
    • Lonhienne, T., C. Gerday, and G. Feller. 2000. Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim. Biophys. Acta. 1543:1-10.
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 1-10
    • Lonhienne, T.1    Gerday, C.2    Feller, G.3
  • 50
    • 0029633168 scopus 로고
    • GROMACS: A message-passing parallel molecular dynamics implementation
    • Berendsen, H. J. C., D. van der Spoel, and R. van Drunen. 1995. GROMACS: a message-passing parallel molecular dynamics implementation. Comput. Phys. Commun. 91:43-56.
    • (1995) Comput. Phys. Commun , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    van der Spoel, D.2    van Drunen, R.3
  • 51
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl, E., B. Hess, and D. van der Spoel. 2001. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J. Mol. Model. 7:306-317.
    • (2001) J. Mol. Model , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 56
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess, B., H. Bekker, H. J. C. Berendsen, and J. G. E. M. Fraaije. 1997. LINCS: a linear constraint solver for molecular simulations. J. Comput. Chem. 18:1463-1472.
    • (1997) J. Comput. Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.G.E.M.4
  • 57
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N Log (N) method for Ewald sums in large systems
    • Darden, T., D. York, and L. Pedersen. 1993. Particle mesh Ewald: an N Log (N) method for Ewald sums in large systems. J. Chem. Phys. 98:1463-1472.
    • (1993) J. Chem. Phys , vol.98 , pp. 1463-1472
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 58
    • 0014216749 scopus 로고
    • A method for the quantitative modification and estimation of carboxylic acid groups in proteins
    • Hoare, D., and D. E. Koshland. 1967. A method for the quantitative modification and estimation of carboxylic acid groups in proteins. J. Biol. Chem. 242:2447-2453.
    • (1967) J. Biol. Chem , vol.242 , pp. 2447-2453
    • Hoare, D.1    Koshland, D.E.2
  • 59
    • 0033672079 scopus 로고    scopus 로고
    • Electrochemical detection of surface hybridization of oligodeoxynucleotides bearing anthraquinone tags at gold electrodes
    • Vilmos Kertesz, V., N. A. Whittemore, G. B. Inamati, M. Manoharan, P. D. Cook, D. C. Baker, and J. Q. Chambers. 2000. Electrochemical detection of surface hybridization of oligodeoxynucleotides bearing anthraquinone tags at gold electrodes. Electroanal. 12:589-594.
    • (2000) Electroanal , vol.12 , pp. 589-594
    • Vilmos Kertesz, V.1    Whittemore, N.A.2    Inamati, G.B.3    Manoharan, M.4    Cook, P.D.5    Baker, D.C.6    Chambers, J.Q.7
  • 61
    • 0034584873 scopus 로고    scopus 로고
    • The use of circular dichroism in the investigation of protein structure and function
    • Kelly, S. M., and N. C. Price. 2000. The use of circular dichroism in the investigation of protein structure and function. Curr. Protein Pept. Sci. 1:349-384.
    • (2000) Curr. Protein Pept. Sci , vol.1 , pp. 349-384
    • Kelly, S.M.1    Price, N.C.2
  • 62
    • 2442703929 scopus 로고    scopus 로고
    • Correlation between functional and structural changes of reduced and oxidized trout hemoglobins I and IV at different pHs. A circular dichroism study
    • Gabbianelli, R., G. Zolese, E. Bertoli, and G. Falcioni. 2004. Correlation between functional and structural changes of reduced and oxidized trout hemoglobins I and IV at different pHs. A circular dichroism study. Eur. J. Biochem. 271:1971-1979.
    • (2004) Eur. J. Biochem , vol.271 , pp. 1971-1979
    • Gabbianelli, R.1    Zolese, G.2    Bertoli, E.3    Falcioni, G.4
  • 63
    • 0027199762 scopus 로고
    • Optical activity of hemoproteins in the Soret region: Circular dichroism of the heme undecapeptide of cytochrome c in aqueous solution
    • Blauer, G., N. Sreerama, and R. W. Woody. 1993. Optical activity of hemoproteins in the Soret region: circular dichroism of the heme undecapeptide of cytochrome c in aqueous solution. Biochemistry. 32:6674-6679.
    • (1993) Biochemistry , vol.32 , pp. 6674-6679
    • Blauer, G.1    Sreerama, N.2    Woody, R.W.3
  • 64
    • 0031972919 scopus 로고    scopus 로고
    • 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation
    • Matulis, D., and R. Lovrien. 1998. 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophys. J. 74:422-429.
    • (1998) Biophys. J , vol.74 , pp. 422-429
    • Matulis, D.1    Lovrien, R.2
  • 65
    • 0023476453 scopus 로고
    • Nile red as a polarity-sensitive fluorescent probe of hydrophobic protein surfaces
    • Sackett, D. L., and J. Wolff. 1987. Nile red as a polarity-sensitive fluorescent probe of hydrophobic protein surfaces. Anal. Biochem. 167:228-234.
    • (1987) Anal. Biochem , vol.167 , pp. 228-234
    • Sackett, D.L.1    Wolff, J.2
  • 67
    • 0021099709 scopus 로고
    • Characterization of the N-demethylation reactions catalyzed by horseradish peroxidase
    • Kedderis, G. L., and P. F. Hollenberg. 1983. Characterization of the N-demethylation reactions catalyzed by horseradish peroxidase. J. Biol. Chem. 258:8129-8138.
    • (1983) J. Biol. Chem , vol.258 , pp. 8129-8138
    • Kedderis, G.L.1    Hollenberg, P.F.2
  • 68
    • 0019321508 scopus 로고
    • The stereochemistry of peroxidase catalysis
    • Poulos, T. L., and J. Kraut. 1980. The stereochemistry of peroxidase catalysis. J. Biol. Chem. 255:8199-8205.
    • (1980) J. Biol. Chem , vol.255 , pp. 8199-8205
    • Poulos, T.L.1    Kraut, J.2


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