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Volumn 1784, Issue 5, 2008, Pages 806-810

Thermodynamic analysis of l-arginine and Nω-hydroxy-l-arginine binding to nitric oxide synthase

Author keywords

Binding; ITC; Nitric oxide synthase; Thermodynamics

Indexed keywords

ARGININE; N(G) HYDROXYARGININE; NITRIC OXIDE SYNTHASE;

EID: 41949139317     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.02.016     Document Type: Article
Times cited : (2)

References (47)
  • 1
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: structure, function and inhibition
    • Alderton W.K., Cooper C.E., and Knowles R.G. Nitric oxide synthases: structure, function and inhibition. Biochem. J. 357 (2001) 593-615
    • (2001) Biochem. J. , vol.357 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 2
    • 0033567065 scopus 로고    scopus 로고
    • Enzymatic function of nitric oxide synthases
    • Andrew P.J., and Mayer B. Enzymatic function of nitric oxide synthases. Cardiovasc. Res. 43 (1999) 521-531
    • (1999) Cardiovasc. Res. , vol.43 , pp. 521-531
    • Andrew, P.J.1    Mayer, B.2
  • 3
    • 0036223475 scopus 로고    scopus 로고
    • Tetrahydrobiopterin in nitric oxide synthesis: a novel biological role for pteridines
    • Gorren A.C.F., and Mayer B. Tetrahydrobiopterin in nitric oxide synthesis: a novel biological role for pteridines. Curr. Drug Metabol. 3 (2002) 133-157
    • (2002) Curr. Drug Metabol. , vol.3 , pp. 133-157
    • Gorren, A.C.F.1    Mayer, B.2
  • 4
    • 0033637918 scopus 로고    scopus 로고
    • Nitric oxide synthase: models and mechanisms
    • Groves J.T., and Wang C.C.Y. Nitric oxide synthase: models and mechanisms. Curr. Opin. Chem. Biol. 4 (2000) 687-695
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 687-695
    • Groves, J.T.1    Wang, C.C.Y.2
  • 5
    • 10444280038 scopus 로고    scopus 로고
    • Structure-function studies on nitric oxide synthases
    • Li H., and Poulos T.L. Structure-function studies on nitric oxide synthases. J. inorg. biochem. 99 (2005) 293-305
    • (2005) J. inorg. biochem. , vol.99 , pp. 293-305
    • Li, H.1    Poulos, T.L.2
  • 6
    • 0033561108 scopus 로고    scopus 로고
    • A new decoration for nitric oxide synthase - a Zn(Cys)(4) site
    • Ludwig M.L., and Marletta M.A. A new decoration for nitric oxide synthase - a Zn(Cys)(4) site. Structure 7 (1999) R73-R79
    • (1999) Structure , vol.7
    • Ludwig, M.L.1    Marletta, M.A.2
  • 7
    • 0033553802 scopus 로고    scopus 로고
    • Nitric oxide: chemical puzzles posed by a biological messenger
    • Pfeiffer S., Mayer B., and Hemmens B. Nitric oxide: chemical puzzles posed by a biological messenger. Angew. Chem., Int. Ed. 38 (1999) 1715-1731
    • (1999) Angew. Chem., Int. Ed. , vol.38 , pp. 1715-1731
    • Pfeiffer, S.1    Mayer, B.2    Hemmens, B.3
  • 8
    • 10444274011 scopus 로고    scopus 로고
    • Ligand-protein interactions in nitric oxide synthase
    • Rousseau D.L., Li D., Couture M., and Yeh S.R. Ligand-protein interactions in nitric oxide synthase. J. Inorg. Biochem. 99 (2005) 306-323
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 306-323
    • Rousseau, D.L.1    Li, D.2    Couture, M.3    Yeh, S.R.4
  • 9
    • 0032930417 scopus 로고    scopus 로고
    • Mammalian nitric oxide synthases
    • Stuehr D.J. Mammalian nitric oxide synthases. Biochim. Biophys. Acta 1411 (1999) 217-230
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 217-230
    • Stuehr, D.J.1
  • 10
    • 4344566972 scopus 로고    scopus 로고
    • Update on mechanism and catalytic regulation in the NO synthases
    • Stuehr D.J., Santolini J., Wang Z.Q., Wei C.C., and Adak S. Update on mechanism and catalytic regulation in the NO synthases. J. Biol. Chem. 279 (2004) 36167-36170
    • (2004) J. Biol. Chem. , vol.279 , pp. 36167-36170
    • Stuehr, D.J.1    Santolini, J.2    Wang, Z.Q.3    Wei, C.C.4    Adak, S.5
  • 11
    • 0034852561 scopus 로고    scopus 로고
    • Formation of a protonated trihydrobiopterin radical cation in the first reaction cycle of neuronal and endothelial nitric oxide synthase detected by electron paramagnetic resonance spectroscopy
    • Schmidt P.P., Lange R., Gorren A.C.F., Werner E.R., Mayer B., and Andersson K.K. Formation of a protonated trihydrobiopterin radical cation in the first reaction cycle of neuronal and endothelial nitric oxide synthase detected by electron paramagnetic resonance spectroscopy. J. Biol. Inorg. Chem. 6 (2001) 151-158
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 151-158
    • Schmidt, P.P.1    Lange, R.2    Gorren, A.C.F.3    Werner, E.R.4    Mayer, B.5    Andersson, K.K.6
  • 12
    • 0037066114 scopus 로고    scopus 로고
    • Reactions catalyzed by the heme domain of inducible nitric oxide synthase: evidence for the involvement of tetrahydrobiopterin in electron transfer
    • Hurshman A.R., and Marletta M.A. Reactions catalyzed by the heme domain of inducible nitric oxide synthase: evidence for the involvement of tetrahydrobiopterin in electron transfer. Biochemistry 41 (2002) 3439-3456
    • (2002) Biochemistry , vol.41 , pp. 3439-3456
    • Hurshman, A.R.1    Marletta, M.A.2
  • 13
    • 1542548514 scopus 로고    scopus 로고
    • Single-turnover of nitric-oxide synthase in the presence of 4-amino-tetrahydrobiopterin - proposed role for tetrahydrobiopterin as a proton donor
    • Sørlie M., Gorren A.C.F., Marchal S., Shimizu T., Lange R., Andersson K.K., and Mayer B. Single-turnover of nitric-oxide synthase in the presence of 4-amino-tetrahydrobiopterin - proposed role for tetrahydrobiopterin as a proton donor. J. Biol. Chem. 278 (2003) 48602-48610
    • (2003) J. Biol. Chem. , vol.278 , pp. 48602-48610
    • Sørlie, M.1    Gorren, A.C.F.2    Marchal, S.3    Shimizu, T.4    Lange, R.5    Andersson, K.K.6    Mayer, B.7
  • 14
    • 0000180763 scopus 로고
    • Temperature dependence of the hydrophobic interaction in protein folding
    • Baldwin R.L. Temperature dependence of the hydrophobic interaction in protein folding. Proc. Natl. Acad. Sci. U.S.A. 83 (1986) 8069-8072
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 8069-8072
    • Baldwin, R.L.1
  • 15
    • 0025906146 scopus 로고
    • Contribution to the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area
    • Livingstone J.R., Spolar R.S., and Record Jr. M.T. Contribution to the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area. Biochemistry 30 (1991) 4237-4244
    • (1991) Biochemistry , vol.30 , pp. 4237-4244
    • Livingstone, J.R.1    Spolar, R.S.2    Record Jr., M.T.3
  • 16
    • 0025098571 scopus 로고
    • Common features of protein unfolding and dissolution of hydrophobic compounds
    • Murphy K.P., Privalov P.L., and Gill S.J. Common features of protein unfolding and dissolution of hydrophobic compounds. Science 247 (1990) 559-561
    • (1990) Science , vol.247 , pp. 559-561
    • Murphy, K.P.1    Privalov, P.L.2    Gill, S.J.3
  • 17
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • Sturtevant J.M. Heat capacity and entropy changes in processes involving proteins. Proc. Natl. Acad. Sci. U.S.A. 74 (1977) 2236-2240
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 2236-2240
    • Sturtevant, J.M.1
  • 18
    • 0029903702 scopus 로고    scopus 로고
    • Interaction of polysaccharides with the N-terminal cellulose-binding domain of Cellulomonas fimi CenC. 1. Binding specificity and calorimetric analysis
    • Tomme P., Creagh A.L., Kilburn D.G., and Haynes C.A. Interaction of polysaccharides with the N-terminal cellulose-binding domain of Cellulomonas fimi CenC. 1. Binding specificity and calorimetric analysis. Biochemistry 35 (1996) 13885-13894
    • (1996) Biochemistry , vol.35 , pp. 13885-13894
    • Tomme, P.1    Creagh, A.L.2    Kilburn, D.G.3    Haynes, C.A.4
  • 20
    • 0029080864 scopus 로고
    • Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin
    • Gomez J., and Freire E. Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin. J. Mol. Biol. 252 (1995) 337-350
    • (1995) J. Mol. Biol. , vol.252 , pp. 337-350
    • Gomez, J.1    Freire, E.2
  • 21
    • 0033550047 scopus 로고    scopus 로고
    • Analysis of the binding of hydroxamic acid and carboxylic acid inhibitors to the stromelysin-1 (matrix metalloproteinase-3) catalytic domain by isothermal titration calorimetry
    • Parker M.H., Lunney E.A., Ortwine D.F., Pavlovsky A.G., Humblet C., and Brouillette C.G. Analysis of the binding of hydroxamic acid and carboxylic acid inhibitors to the stromelysin-1 (matrix metalloproteinase-3) catalytic domain by isothermal titration calorimetry. Biochemistry 38 (1999) 13592-13601
    • (1999) Biochemistry , vol.38 , pp. 13592-13601
    • Parker, M.H.1    Lunney, E.A.2    Ortwine, D.F.3    Pavlovsky, A.G.4    Humblet, C.5    Brouillette, C.G.6
  • 22
    • 6444235533 scopus 로고    scopus 로고
    • Thermodynamic characterization of the binding of tetrahydropterins to phenylalanine hydroxylase
    • Pey A.L., Thorolfsson M., Teigen K., Ugarte M., and Martinez A. Thermodynamic characterization of the binding of tetrahydropterins to phenylalanine hydroxylase. J. Am. Chem. Soc. 126 (2004) 13670-13678
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 13670-13678
    • Pey, A.L.1    Thorolfsson, M.2    Teigen, K.3    Ugarte, M.4    Martinez, A.5
  • 23
    • 0031547981 scopus 로고    scopus 로고
    • Dissecting the energetics of a protein-protein interaction: the binding of ovomucoid third domain to elastase
    • Baker B.M., and Murphy K.P. Dissecting the energetics of a protein-protein interaction: the binding of ovomucoid third domain to elastase. J. Mol. Biol. 268 (1997) 557-569
    • (1997) J. Mol. Biol. , vol.268 , pp. 557-569
    • Baker, B.M.1    Murphy, K.P.2
  • 24
    • 0035839435 scopus 로고    scopus 로고
    • Intra-subunit and Inter-subunit electron transfer in neuronal nitric-oxide synthase. Effect of calmodulin on heterodimer catalysis
    • Sagami I., Daff S., and Shimizu T. Intra-subunit and Inter-subunit electron transfer in neuronal nitric-oxide synthase. Effect of calmodulin on heterodimer catalysis. J. Biol. Chem. 276 (2001) 30036-30042
    • (2001) J. Biol. Chem. , vol.276 , pp. 30036-30042
    • Sagami, I.1    Daff, S.2    Shimizu, T.3
  • 25
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman T., Williston S., Brandts J.F., and Lin L.N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179 (1989) 131-137
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 26
    • 0028085986 scopus 로고
    • Hydration and convergence temperatures - on the use and interpretation of correlation plots
    • Murphy K.P. Hydration and convergence temperatures - on the use and interpretation of correlation plots. Biophys. Chem. 51 (1994) 311-326
    • (1994) Biophys. Chem. , vol.51 , pp. 311-326
    • Murphy, K.P.1
  • 28
    • 41949133829 scopus 로고    scopus 로고
    • Gurney, R. W. Ionic Processes in Solution, McGraw-Hill, New York, 193.
    • Gurney, R. W. Ionic Processes in Solution, McGraw-Hill, New York, 193.
  • 29
    • 0028228418 scopus 로고
    • The entropic cost of bound water in crystals and biomolecules
    • Dunitz J.D. The entropic cost of bound water in crystals and biomolecules. Science 264 (1994) 670
    • (1994) Science , vol.264 , pp. 670
    • Dunitz, J.D.1
  • 30
    • 0027441142 scopus 로고
    • Macrophage nitric oxide synthase subunits. Purification, characterization, and role of prosthetic groups and substrate in regulating their association into a dimeric enzyme
    • Baek K.J., Thiel B.A., Lucas S., and Stuehr D.J. Macrophage nitric oxide synthase subunits. Purification, characterization, and role of prosthetic groups and substrate in regulating their association into a dimeric enzyme. J. Biol. Chem. 268 (1993) 21120-21129
    • (1993) J. Biol. Chem. , vol.268 , pp. 21120-21129
    • Baek, K.J.1    Thiel, B.A.2    Lucas, S.3    Stuehr, D.J.4
  • 31
    • 0029664605 scopus 로고    scopus 로고
    • Domains of macrophage NO synthase have divergent roles in forming and stabilizing the active dimeric enzyme
    • Ghosh D.K., bu-Soud H.M., and Stuehr D.J. Domains of macrophage NO synthase have divergent roles in forming and stabilizing the active dimeric enzyme. Biochemistry 35 (1996) 1444-1449
    • (1996) Biochemistry , vol.35 , pp. 1444-1449
    • Ghosh, D.K.1    bu-Soud, H.M.2    Stuehr, D.J.3
  • 32
    • 0029125762 scopus 로고
    • Structural analysis of porcine brain nitric oxide synthase reveals a role for tetrahydrobiopterin and l-arginine in the formation of an SDS-resistant dimer
    • Klatt P., Schmidt K., Lehner D., Glatter O., Bachinger H.P., and Mayer B. Structural analysis of porcine brain nitric oxide synthase reveals a role for tetrahydrobiopterin and l-arginine in the formation of an SDS-resistant dimer. EMBO J. 14 (1995) 3687-3695
    • (1995) EMBO J. , vol.14 , pp. 3687-3695
    • Klatt, P.1    Schmidt, K.2    Lehner, D.3    Glatter, O.4    Bachinger, H.P.5    Mayer, B.6
  • 33
    • 0031030864 scopus 로고    scopus 로고
    • Subunit interactions of endothelial nitric-oxide synthase. Comparisons to the neuronal and inducible nitric-oxide synthase isoforms
    • Venema R.C., Ju H., Zou R., Ryan J.W., and Venema V.J. Subunit interactions of endothelial nitric-oxide synthase. Comparisons to the neuronal and inducible nitric-oxide synthase isoforms. J. Biol. Chem. 272 (1997) 1276-1282
    • (1997) J. Biol. Chem. , vol.272 , pp. 1276-1282
    • Venema, R.C.1    Ju, H.2    Zou, R.3    Ryan, J.W.4    Venema, V.J.5
  • 34
    • 0029975203 scopus 로고    scopus 로고
    • Analysis of substrate-induced electronic, catalytic, and structural changes in inducible NO synthase
    • Sennequier N., and Stuehr D.J. Analysis of substrate-induced electronic, catalytic, and structural changes in inducible NO synthase. Biochemistry 35 (1996) 5883-5892
    • (1996) Biochemistry , vol.35 , pp. 5883-5892
    • Sennequier, N.1    Stuehr, D.J.2
  • 35
    • 0033592424 scopus 로고    scopus 로고
    • Stopped-flow analysis of substrate binding to neuronal nitric oxide synthase
    • Abu-Soud H.M., Wang J., Rousseau D.L., and Stuehr D.J. Stopped-flow analysis of substrate binding to neuronal nitric oxide synthase. Biochemistry 38 (1999) 12446-12451
    • (1999) Biochemistry , vol.38 , pp. 12446-12451
    • Abu-Soud, H.M.1    Wang, J.2    Rousseau, D.L.3    Stuehr, D.J.4
  • 36
    • 0027442932 scopus 로고
    • Optical difference spectrophotometry as a probe of rat brain nitric oxide synthase heme-substrate interaction
    • McMillan K., and Masters B.S.S. Optical difference spectrophotometry as a probe of rat brain nitric oxide synthase heme-substrate interaction. Biochemistry 32 (1993) 9875-9880
    • (1993) Biochemistry , vol.32 , pp. 9875-9880
    • McMillan, K.1    Masters, B.S.S.2
  • 37
    • 0034791669 scopus 로고    scopus 로고
    • Titration of low K(d) binding sites: binding of arginine analogs to nitric oxide synthases
    • Smith S.M., Sham C., Roman L., Martasek P., and Salerno J.C. Titration of low K(d) binding sites: binding of arginine analogs to nitric oxide synthases. Nitric Oxide 5 (2001) 442-452
    • (2001) Nitric Oxide , vol.5 , pp. 442-452
    • Smith, S.M.1    Sham, C.2    Roman, L.3    Martasek, P.4    Salerno, J.C.5
  • 38
    • 0037129974 scopus 로고    scopus 로고
    • Binding of l-arginine and imidazole suggests heterogeneity of rat brain neuronal nitric oxide synthase
    • Gorren A.C.F., Schmidt K., and Mayer B. Binding of l-arginine and imidazole suggests heterogeneity of rat brain neuronal nitric oxide synthase. Biochemistry 41 (2002) 7819-7829
    • (2002) Biochemistry , vol.41 , pp. 7819-7829
    • Gorren, A.C.F.1    Schmidt, K.2    Mayer, B.3
  • 39
    • 21344458345 scopus 로고    scopus 로고
    • Relationship between the structure of guanidines and N-hydroxyguanidines, their binding to inducible nitric oxide synthase (iNOS) and their iNOS-catalysed oxidation to NO
    • Lefevre-Groboillot D., Boucher J.L., Stuehr D.J., and Mansuy D. Relationship between the structure of guanidines and N-hydroxyguanidines, their binding to inducible nitric oxide synthase (iNOS) and their iNOS-catalysed oxidation to NO. FEBS J. 272 (2005) 3172-3183
    • (2005) FEBS J. , vol.272 , pp. 3172-3183
    • Lefevre-Groboillot, D.1    Boucher, J.L.2    Stuehr, D.J.3    Mansuy, D.4
  • 40
    • 18744415136 scopus 로고    scopus 로고
    • The novel binding mode of N-alkyl-N′-hydroxyguanidine to neuronal nitric oxide synthase provides mechanistic insights into NO biosynthesis
    • Li H., Shimizu H., Flinspach M., Jamal J., Yang W., Xian M., Cai T., Wen E.Z., Jia Q., Wang P.G., and Poulos T.L. The novel binding mode of N-alkyl-N′-hydroxyguanidine to neuronal nitric oxide synthase provides mechanistic insights into NO biosynthesis. Biochemistry 41 (2002) 13868-13875
    • (2002) Biochemistry , vol.41 , pp. 13868-13875
    • Li, H.1    Shimizu, H.2    Flinspach, M.3    Jamal, J.4    Yang, W.5    Xian, M.6    Cai, T.7    Wen, E.Z.8    Jia, Q.9    Wang, P.G.10    Poulos, T.L.11
  • 42
    • 33646357912 scopus 로고    scopus 로고
    • Conformational flexibility of mammalian cytochrome P4502B4 in binding imidazole inhibitors with different ring chemistry and side chains - solution thermodynamics and molecular modeling
    • Muralidhara B.K., Negi S., Chin C.C., Braun W., and Halpert J.R. Conformational flexibility of mammalian cytochrome P4502B4 in binding imidazole inhibitors with different ring chemistry and side chains - solution thermodynamics and molecular modeling. J. Biol. Chem. 281 (2006) 8051-8061
    • (2006) J. Biol. Chem. , vol.281 , pp. 8051-8061
    • Muralidhara, B.K.1    Negi, S.2    Chin, C.C.3    Braun, W.4    Halpert, J.R.5
  • 43
    • 34948839893 scopus 로고    scopus 로고
    • Heat capacity changes in heme protein-ligand interactions
    • Zakariassen H., and Sørlie M. Heat capacity changes in heme protein-ligand interactions. Thermochim. Acta 464 (2007) 24-28
    • (2007) Thermochim. Acta , vol.464 , pp. 24-28
    • Zakariassen, H.1    Sørlie, M.2
  • 44
    • 0000866128 scopus 로고
    • Hydrophobic effect in protein folding and other noncovalent processes involving proteins
    • Spolar R.S., Ha J.H., and Record M.T. Hydrophobic effect in protein folding and other noncovalent processes involving proteins. Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 8382-8385
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 8382-8385
    • Spolar, R.S.1    Ha, J.H.2    Record, M.T.3
  • 45
    • 0032774244 scopus 로고    scopus 로고
    • Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an X-ray crystallographic study
    • Bolognesi M., Rosano C., Losso R., Borassi A., Rizzi M., Wittenberg J.B., Boffi A., and Ascenzi P. Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an X-ray crystallographic study. Biophys. J. 77 (1999) 1093-1099
    • (1999) Biophys. J. , vol.77 , pp. 1093-1099
    • Bolognesi, M.1    Rosano, C.2    Losso, R.3    Borassi, A.4    Rizzi, M.5    Wittenberg, J.B.6    Boffi, A.7    Ascenzi, P.8
  • 46
    • 0026022973 scopus 로고
    • X-ray crystal-structure of the ferric sperm whale myoglobin-imidazole complex at 2.0 Å resolution
    • Lionetti C., Guanziroli M.G., Frigerio F., Ascenzi P., and Bolognesi M. X-ray crystal-structure of the ferric sperm whale myoglobin-imidazole complex at 2.0 Å resolution. J. Mol. Biol. 217 (1991) 409-412
    • (1991) J. Mol. Biol. , vol.217 , pp. 409-412
    • Lionetti, C.1    Guanziroli, M.G.2    Frigerio, F.3    Ascenzi, P.4    Bolognesi, M.5
  • 47
    • 0032524204 scopus 로고    scopus 로고
    • Structural and spectroscopic studies of azide complexes of horse heart myoglobin and the His-64 -> Thr variant
    • Maurus R., Bogumil R., Nguyen N.T., Mauk A.G., and Brayer G. Structural and spectroscopic studies of azide complexes of horse heart myoglobin and the His-64 -> Thr variant. Biochem. J. 332 (1998) 67-74
    • (1998) Biochem. J. , vol.332 , pp. 67-74
    • Maurus, R.1    Bogumil, R.2    Nguyen, N.T.3    Mauk, A.G.4    Brayer, G.5


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