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Volumn 48, Issue 18, 2009, Pages 3864-3876

Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthase

Author keywords

[No Author keywords available]

Indexed keywords

BOUND STATE; CATALYTIC BEHAVIOR; CITRULLINE; CONFORMATIONAL EQUILIBRIUM; CONFORMATIONAL STATE; ELECTRON PARAMAGNETIC RESONANCE; ELECTRON TRANSFER; EQUILIBRIUM MODELS; L-ARGININE; NITRIC OXIDE SYNTHASES; NITRIC-OXIDE SYNTHASE; OXYGENASE; REDOX STATE; SET-POINT; SPECTROSCOPIC TECHNIQUE; STOPPED FLOW; SUBDOMAIN; UNBOUND STATE;

EID: 66149139413     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8021087     Document Type: Article
Times cited : (46)

References (85)
  • 1
    • 2342482002 scopus 로고    scopus 로고
    • Nitric oxide in health and disease of the respiratory system
    • DOI 10.1152/physrev.00034.2003
    • Ricciardolo, F. L., Sterk, P. J., Gaston, B., and Folkerts, G. (2004) Nitric oxide in health and disease of the respiratory system. Physiol. Rev. 84, 731-765. (Pubitemid 38823765)
    • (2004) Physiological Reviews , vol.84 , Issue.3 , pp. 731-765
    • Ricciardolo, F.L.M.1    Sterk, P.J.2    Gaston, B.3    Folkerts, G.4
  • 2
    • 28044467552 scopus 로고    scopus 로고
    • Recent advances in the understanding of the role of nitric oxide in cardiovascular homeostasis
    • DOI 10.1016/j.pharmthera.2005.04.005, PII S0163725805000811
    • Schulz, R., Rassaf, T., Massion, P. B., Kelm, M., and Balligand, J.L. (2005) Recent advances in the understanding of the role of nitric oxide in cardiovascular homeostasis. Pharmacol. Ther. 108, 225-256. (Pubitemid 41691866)
    • (2005) Pharmacology and Therapeutics , vol.108 , Issue.3 , pp. 225-256
    • Schulz, R.1    Rassaf, T.2    Massion, P.B.3    Kelm, M.4    Balligand, J.-L.5
  • 3
    • 18844362885 scopus 로고    scopus 로고
    • Regulation of endothelial derived nitric oxide in health and disease
    • Sessa, W. C. (2005) Regulation of endothelial derived nitric oxide in health and disease. Mem. Inst. Oswaldo Cruz 100 (Suppl. 1), 15-18. (Pubitemid 40685434)
    • (2005) Memorias Do Instituto Oswaldo Cruz , vol.100 , Issue.SUPPL. 1 , pp. 15-18
    • Sessa, W.C.1
  • 4
    • 58849147441 scopus 로고    scopus 로고
    • Nitric oxide in health and disease of the nervous system
    • Knott, A. B., and Bossy-Wetzel, E. (2009) Nitric oxide in health and disease of the nervous system. Antioxid. Redox Signaling 11, 541-554.
    • (2009) Antioxid. Redox Signaling , vol.11 , pp. 541-554
    • Knott, A.B.1    Bossy-Wetzel, E.2
  • 5
    • 0032930417 scopus 로고    scopus 로고
    • Mammalian nitric oxide synthases
    • DOI 10.1016/S0005-2728(99)00016-X, PII S000527289900016X
    • Stuehr, D. J. (1999) Mammalian nitric oxide synthases. Biochim. Biophys. Acta 1411, 217-230. (Pubitemid 29221951)
    • (1999) Biochimica et Biophysica Acta - Bioenergetics , vol.1411 , Issue.2-3 , pp. 217-230
    • Stuehr, D.J.1
  • 6
    • 10444280038 scopus 로고    scopus 로고
    • Structure-function studies on nitric oxide synthases
    • DOI 10.1016/j.jinorgbio.2004.10.016, PII S0162013404003216, Heme-Diatomic Interactions, Part 1
    • Li, H., and Poulos, T. L. (2005) Structure-function studies on nitric oxide synthases. J. Inorg. Biochem. 99, 293-305. (Pubitemid 39642983)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 293-305
    • Li, H.1    Poulos, T.L.2
  • 7
    • 0032571411 scopus 로고    scopus 로고
    • Structure of nitric oxide synthase oxygenase dimer with pterin and substrate
    • DOI 10.1126/science.279.5359.2121
    • Crane, B. R., Arvai, A. S., Ghosh, D. K., Wu, C., Getzoff, E. D., Stuehr, D. J., and Tainer, J. A. (1998) Structure of nitric oxide synthase oxygenase dimer with pterin and substrate. Science 279, 2121-2126. (Pubitemid 28196359)
    • (1998) Science , vol.279 , Issue.5359 , pp. 2121-2126
    • Crane, B.R.1    Arvai, A.S.2    Ghosh, D.K.3    Wu, C.4    Getzoff, E.D.5    Stuehr, D.J.6    Tainer, J.A.7
  • 8
    • 0035813091 scopus 로고    scopus 로고
    • Crystal structure of the FAD/NADPH-binding domain of rat neuronal nitric-oxide synthase. Comparisons with NADPH-cytochrome P450 oxidoreductase
    • Zhang, J., Martasek, P., Paschke, R., Shea, T., Masters, B. S. S., and Kim, J. J. (2001) Crystal structure of the FAD/NADPH-binding domain of rat neuronal nitric-oxide synthase. Comparisons with NADPH-cytochrome P450 oxidoreductase. J. Biol. Chem. 276, 37506-37513.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37506-37513
    • Zhang, J.1    Martasek, P.2    Paschke, R.3    Shea, T.4    Masters, B.S.S.5    Kim, J.J.6
  • 9
    • 0037163086 scopus 로고    scopus 로고
    • Distinct dimer interaction and regulation in nitric-oxide synthase types I, II, and III
    • Panda, K., Rosenfeld, R. J., Ghosh, S., Meade, A. L., Getzoff, E. D., and Stuehr, D. J. (2002) Distinct dimer interaction and regulation in nitric-oxide synthase types I, II, and III. J. Biol. Chem. 277 31020-31030.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31020-31030
    • Panda, K.1    Rosenfeld, R.J.2    Ghosh, S.3    Meade, A.L.4    Getzoff, E.D.5    Stuehr, D.J.6
  • 10
    • 0036797554 scopus 로고    scopus 로고
    • Stopped-flow kinetic studies of electron transfer in the reductase domain of neuronal nitric oxide synthase: Re-evaluation of the kinetic mechanism reveals new enzyme intermediates and variation with cytochrome P450 reductase
    • DOI 10.1042/BJ20020667
    • Knight, K., and Scrutton, N. S. (2002) Stopped-flow kinetic studies of electron transfer in the reductase domain of neuronal nitric oxide synthase: re-evaluation of the kinetic mechanism reveals new enzyme intermediates and variation with cytochrome P450 reductase. Biochem. J. 367, 19-30. (Pubitemid 35176887)
    • (2002) Biochemical Journal , vol.367 , Issue.1 , pp. 19-30
    • Knight, K.1    Scrutton, N.S.2
  • 11
    • 0036548323 scopus 로고    scopus 로고
    • Intrinsic and extrinsic modulation of nitric oxide synthase activity
    • DOI 10.1021/cr000661e
    • Roman, L. J., Martasek, P., and Masters, B. S. (2002) Intrinsic and extrinsic modulation of nitric oxide synthase activity. Chem. Rev. 102, 1179-1190. (Pubitemid 35377608)
    • (2002) Chemical Reviews , vol.102 , Issue.4 , pp. 1179-1189
    • Roman, L.J.1    Martasek, P.2    Masters, B.S.S.3
  • 12
    • 0037527802 scopus 로고    scopus 로고
    • Calmodulin-dependent regulation of mammalian nitric oxide synthase
    • DOI 10.1042/BST0310502
    • Daff, S. (2003) Calmodulin-dependent regulation of mammalian nitric oxide synthase. Biochem. Soc. Trans. 31, 502-505. (Pubitemid 36750720)
    • (2003) Biochemical Society Transactions , vol.31 , Issue.3 , pp. 502-505
    • Daff, S.1
  • 14
    • 3042543913 scopus 로고    scopus 로고
    • Thermodynamic and kinetic analysis of the isolated FAD domain of rat neuronal nitric oxide synthase altered in the region of the FAD shielding residue Phe1395
    • DOI 10.1111/j.1432-1033.2004.04185.x
    • Dunford, A. J., Marshall, K. R., Munro, A. W., and Scrutton, N. S. (2004) Thermodynamic and kinetic analysis of the isolated FAD domain of rat neuronal nitric oxide synthase altered in the region of the FAD shielding residue Phe1395. Eur. J. Biochem. 271, 2548-2560. (Pubitemid 38813585)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.12 , pp. 2548-2560
    • Dunford, A.J.1    Marshall, K.R.2    Munro, A.W.3    Scrutton, N.S.4
  • 15
    • 4644273566 scopus 로고    scopus 로고
    • Redox properties of the isolated flavin mononucleotide- and flavin adenine dinucleotide-binding domains of neuronal nitric oxide synthase
    • DOI 10.1021/bi049312v
    • Garnaud, P. E., Koetsier, M., Ost, T. W., and Daff, S. (2004) Redox properties of the isolated flavin mononucleotide- and flavin adenine dinucleotide-binding domains of neuronal nitric oxide synthase. Biochemistry 43, 11035-11044. (Pubitemid 39433692)
    • (2004) Biochemistry , vol.43 , Issue.34 , pp. 11035-11044
    • Garnaud, P.E.1    Koetsier, M.2    Ost, T.W.B.3    Daff, S.4
  • 17
    • 12544253945 scopus 로고    scopus 로고
    • Thermodynamic and kinetic analysis of the nitrosyl, carbonyl, and dioxy heme complexes of neuronal nitric-oxide synthase. the roles of substrate and tetrahydrobiopterin in oxygen activation
    • Ost, T. W., and Daff, S. (2005) Thermodynamic and kinetic analysis of the nitrosyl, carbonyl, and dioxy heme complexes of neuronal nitric-oxide synthase. The roles of substrate and tetrahydrobiopterin in oxygen activation. J. Biol. Chem. 280, 965-973.
    • (2005) J. Biol. Chem. , vol.280 , pp. 965-973
    • Ost, T.W.1    Daff, S.2
  • 18
    • 33747335659 scopus 로고    scopus 로고
    • Electron transfer by neuronal nitric-oxide synthase is regulated by concerted interaction of calmodulin and two intrinsic regulatory elements
    • DOI 10.1074/jbc.M603671200
    • Roman, L. J., and Masters, B. S. (2006) Electron transfer by neuronal nitric oxide synthase is regulated by concerted interaction of calmodulin and two intrinsic regulatory elements. J. Biol. Chem. 281, 23111-23118. (Pubitemid 44242343)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.32 , pp. 23111-23118
    • Roman, L.J.1    Masters, B.S.S.2
  • 19
    • 37249008118 scopus 로고    scopus 로고
    • Versatile regulation of neuronal nitric oxide synthase by specific regions of its C-terminal tail
    • DOI 10.1021/bi701646k
    • Tiso, M., Tejero, J., Panda, K., Aulak, K. S, and Stuehr, D. J. (2007) Versatile regulation of neuronal nitric oxide synthase by specific regions of its C-terminal tail. Biochemistry 46, 14418-14428. (Pubitemid 350276349)
    • (2007) Biochemistry , vol.46 , Issue.50 , pp. 14418-14428
    • Tiso, M.1    Tejero, J.2    Panda, K.3    Aulak, K.S.4    Stuehr, D.J.5
  • 20
    • 34247626781 scopus 로고    scopus 로고
    • Conformational and thermodynamic control of electron transfer in neuronal nitric oxide synthase
    • DOI 10.1021/bi7001339
    • Dunford, A. J., Rigby, S. E. J., Hay, S., Munro, A. W., and Scrutton, N. S. (2007) Conformational and thermodynamic control of electron transfer in neuronal nitric oxide synthase. Biochemistry 46, 5018-5029. (Pubitemid 46683000)
    • (2007) Biochemistry , vol.46 , Issue.17 , pp. 5018-5029
    • Dunford, A.J.1    Rigby, S.E.J.2    Hay, S.3    Munro, A.W.4    Scrutton, N.S.5
  • 21
    • 34447570813 scopus 로고    scopus 로고
    • Differential binding of calmodulin domains to constitutive and inducible nitric oxide synthase enzymes
    • DOI 10.1021/bi062130b
    • Spratt, D. E., Taiakina, V., Palmer, M., and Guillemette, J. G. (2007) Differential binding of calmodulin domains to constitutive and inducible nitric oxide synthase enzymes. Biochemistry 46, 8288-8300. (Pubitemid 47075968)
    • (2007) Biochemistry , vol.46 , Issue.28 , pp. 8288-8300
    • Spratt, D.E.1    Taiakina, V.2    Palmer, M.3    Guillemette, J.G.4
  • 22
    • 5444247065 scopus 로고    scopus 로고
    • Redox function of tetrahydrobiopterin and effect of L-arginine on oxygen binding in endothelial nitric oxide synthase
    • DOI 10.1021/bi049026j
    • Berka, V., Yeh, H. C., Gao, D., Kiran, F., and Tsai, A. L. (2004) Redox function of tetrahydrobiopterin and effect of L-arginine on oxygen binding in endothelial nitric oxide synthase. Biochemistry 43, 13137-13148. (Pubitemid 39362782)
    • (2004) Biochemistry , vol.43 , Issue.41 , pp. 13137-13148
    • Berka, V.1    Yeh, H.-C.2    Gao, D.3    Kiran, F.4    Tsai, A.-L.5
  • 23
    • 3543042462 scopus 로고    scopus 로고
    • Three different oxygen-induced radical species in endothelial nitric-oxide synthase oxygenase domain under regulation by L-arginine and tetrahydrobiopterin
    • DOI 10.1074/jbc.M404044200
    • Berka, V., Wu, G., Yeh, H. C., Palmer, G., and Tsai, A. L. (2004) Three different oxygen-induced radical species in endothelial nitricoxide synthase oxygenase domain under regulation by L-arginine and tetrahydrobiopterin. J. Biol. Chem. 279, 32243-32251. (Pubitemid 39014673)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.31 , pp. 32243-32251
    • Berka, V.1    Wu, G.2    Yeh, H.-C.3    Palmer, G.4    Tsai, A.-L.5
  • 24
    • 0345505668 scopus 로고    scopus 로고
    • Determination of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1
    • DOI 10.1046/j.1432-1033.2003.03474.x
    • Finn, R. D., Basran, J., Roitel, O., Wolf, C. R., Munro, A. W., Paine, M. J., and Scrutton, N. S. (2003) Determination of the redox potentials and electron transfer properties of the FAD- and FMN-binding domains of the human oxidoreductase NR1. Eur. J. Biochem. 270, 1164-1175. (Pubitemid 36384449)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.6 , pp. 1164-1175
    • Finn, R.D.1    Basran, J.2    Roitel, O.3    Wolf, C.R.4    Munro, A.W.5    Paine, M.J.I.6    Scrutton, N.S.7
  • 27
    • 34250194018 scopus 로고    scopus 로고
    • Protein interactions in the human methionine synthase-methionine synthase reductase complex and implications for the mechanism of enzyme reactivation
    • DOI 10.1021/bi700339v
    • Wolthers, K. R., and Scrutton, N. S. (2007) Protein interactions in the human methionine synthase-methionine synthase reductase complex and implications for the mechanism of enzyme reactivation. Biochemistry 46, 6696-6709. (Pubitemid 46906401)
    • (2007) Biochemistry , vol.46 , Issue.23 , pp. 6696-6709
    • Wolthers, K.R.1    Scrutton, N.S.2
  • 28
    • 0034733026 scopus 로고    scopus 로고
    • Association of cytochromes P450 with their reductases: Opposite sign of the electrostatic interactions in P450BM-3 as compared with the microsomal 2B4 system
    • DOI 10.1021/bi992936u
    • Davydov, D. R., Kariakin, A. A., Petushkova, N. A., and Peterson, J. A. (2000) Association of cytochromes P450 with their reductases: opposite sign of the electrostatic interactions in P450BM-3 as compared with the microsomal 2B4 system. Biochemistry 39, 6489-6497. (Pubitemid 30347155)
    • (2000) Biochemistry , vol.39 , Issue.21 , pp. 6489-6497
    • Davydov, D.R.1    Kariakin, A.A.2    Petushkova, N.A.3    Peterson, J.A.4
  • 29
    • 35448960897 scopus 로고    scopus 로고
    • Obligatory intermolecular electron-transfer from FAD to FMN in dimeric P450BM-3
    • DOI 10.1021/bi701031r
    • Kitazume, T., Haines, D. C., Estabrook, R. W., Chen, B., and Peterson, J. A. (2007) Obligatory intermolecular electron-transfer from FAD to FMN in dimeric P450BM-3. Biochemistry 46 11892-11901. (Pubitemid 47623757)
    • (2007) Biochemistry , vol.46 , Issue.42 , pp. 11892-11901
    • Kitazume, T.1    Haines, D.C.2    Estabrook, R.W.3    Chen, B.4    Peterson, J.A.5
  • 30
    • 0034535502 scopus 로고    scopus 로고
    • A simplifed functional version of the Escherichia coli sulfite reductase
    • DOI 10.1074/jbc.M005619200
    • Zeghouf, M., Fontecave, M., and Coves, J. (2000) A simplifed functional version of the Escherichia coli sulfite reductase. J. Biol. Chem. 275, 37651-37656. (Pubitemid 32004877)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.48 , pp. 37651-37656
    • Zeghouf, M.1    Fontecave, M.2    Coves, J.3
  • 31
    • 0029095516 scopus 로고
    • The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure
    • Eschenbrenner, M., Coves, J., and Fontecave, M. (1995) The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure. J. Biol. Chem. 270, 20550-20555.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20550-20555
    • Eschenbrenner, M.1    Coves, J.2    Fontecave, M.3
  • 32
    • 0035929601 scopus 로고    scopus 로고
    • Human Methionine Synthase Reductase, a Soluble P-450 Reductase-like Dual Flavoprotein, is Sufficient for NADPH-dependent Methionine Synthase Activation
    • DOI 10.1074/jbc.M103707200
    • Olteanu, H., and Banerjee, R. (2001) Human methionine synthase reductase, a soluble P-450 reductase-like dual flavoprotein, is sufficient for NADPH-dependent methionine synthase activation. J. Biol. Chem. 276, 35558-35563. (Pubitemid 37384355)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.38 , pp. 35558-35563
    • Olteanu, H.1    Banerjee, R.2
  • 33
    • 0026023225 scopus 로고
    • + reductase: Prototype for a structurally novel flavoenzyme family
    • Karplus, P. A., Daniels, M. J., and Herriott, J. R. (1991) Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family. Science 251, 60-66. (Pubitemid 21916851)
    • (1991) Science , vol.251 , Issue.4989 , pp. 60-66
    • Karplus, P.A.1    Daniels, M.J.2    Herriott, J.R.3
  • 34
    • 0031038029 scopus 로고    scopus 로고
    • + reductases: A basal structural framework and a multiplicity of functions
    • Arakaki, A. K., Ceccarelli, E. A., and Carrillo, N. (1997) Plant-type ferredoxin-NADP+ reductases: a basal structural framework and a multiplicity of functions. FASEB J. 11, 133-140. (Pubitemid 27097586)
    • (1997) FASEB Journal , vol.11 , Issue.2 , pp. 133-140
    • Arakaki, A.K.1    Ceccarelli, E.A.2    Carrillo, N.3
  • 35
    • 0038368151 scopus 로고    scopus 로고
    • + reductase catalytic mechanism
    • DOI 10.1046/j.1432-1033.2003.03566.x
    • Carrillo, N., and Ceccarelli, E. A. (2003) Open questions in ferredoxin- NADP+ reductase catalytic mechanism. Eur. J. Biochem. 270, 1900-1915. (Pubitemid 36560810)
    • (2003) European Journal of Biochemistry , vol.270 , Issue.9 , pp. 1900-1915
    • Carrillo, N.1    Ceccarelli, E.A.2
  • 36
    • 33646052947 scopus 로고    scopus 로고
    • Flavodoxins: Sequence, folding, binding, function and beyond
    • Sancho, J. (2006) Flavodoxins: sequence, folding, binding, function and beyond. Cell. Mol. Life Sci. 63, 855-864.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 855-864
    • Sancho, J.1
  • 37
    • 51849113324 scopus 로고    scopus 로고
    • Importance of the domain-domain interface to the catalytic action of the NO synthase reductase domain
    • Welland, A., Garnaud, P. E., Kitamura, M., Miles, C. S., and Daff, S. (2008) Importance of the domain-domain interface to the catalytic action of the NO synthase reductase domain. Biochemistry 47, 9771-9780.
    • (2008) Biochemistry , vol.47 , pp. 9771-9780
    • Welland, A.1    Garnaud, P.E.2    Kitamura, M.3    Miles, C.S.4    Daff, S.5
  • 38
  • 39
    • 50349102696 scopus 로고    scopus 로고
    • Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitricoxide synthase flavoproteins
    • Ilagan, R. P., Tiso, M., Konas, D. W., Hemann, C., Durra, D., Hille, R., and Stuehr, D. J. (2008) Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitricoxide synthase flavoproteins. J. Biol. Chem. 283, 19603-19615.
    • (2008) J. Biol. Chem. , vol.283 , pp. 19603-19615
    • Ilagan, R.P.1    Tiso, M.2    Konas, D.W.3    Hemann, C.4    Durra, D.5    Hille, R.6    Stuehr, D.J.7
  • 40
    • 28244474850 scopus 로고    scopus 로고
    • 1400 enables NADPH to regulate electron transfer in neuronal nitric-oxide synthase
    • DOI 10.1074/jbc.M507775200
    • Tiso, M., Konas, D. W., Panda, K., Garcin, E. D., Sharma, M., Getzoff, E. D., and Stuehr, D. J. (2005) C-terminal tail residue Arg1400 enables NADPH to regulate electron transfer in neuronal nitric-oxide synthase. J. Biol. Chem. 280, 39208-39219. (Pubitemid 41713873)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39208-39219
    • Tiso, M.1    Konas, D.W.2    Panda, K.3    Garcin, E.D.4    Sharma, M.5    Getzoff, E.D.6    Stuehr, D.J.7
  • 41
    • 0037072782 scopus 로고    scopus 로고
    • Calmodulin activates electron transfer through neuronal nitric-oxide synthase reductase domain by releasing an NADPH-dependent conformational lock
    • Craig, D. H., Chapman, S. K., and Daff, S. (2002) Calmodulin activates electron transfer through neuronal nitric-oxide synthase reductase domain by releasing an NADPH-dependent conformational lock. J. Biol. Chem. 277, 33987-33994.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33987-33994
    • Craig, D.H.1    Chapman, S.K.2    Daff, S.3
  • 42
    • 34247863706 scopus 로고    scopus 로고
    • Direct measurement by laser flash photolysis of intraprotein electron transfer in a rat neuronal nitric oxide synthase
    • DOI 10.1021/ja068685b
    • Feng, C. J., Tollin, G., Hazzard, J. T., Nahm, N. J., Guillemette, J. G., Salerno, J. C., and Ghosh, D. K. (2007) Direct measurement by laser flash photolysis of intraprotein electron transfer in a rat neuronal nitric oxide synthase. J. Am. Chem. Soc. 129, 5621-5629. (Pubitemid 46697651)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.17 , pp. 5621-5629
    • Feng, C.1    Tollin, G.2    Hazzard, J.T.3    Nahm, N.J.4    Guillemette, J.G.5    Salerno, J.C.6    Ghosh, D.K.7
  • 43
    • 32244437847 scopus 로고    scopus 로고
    • Global effects of the energetics of coenzyme binding: NADPH controls the protein interaction properties of human cytochrome P450 reductase
    • DOI 10.1021/bi052115r
    • Grunau, A., Paine, M. J., Ladbury, J. E., and Gutierrez, A. (2006) Global effects of the energetics of coenzyme binding: NADPH controls the protein interaction properties of human cytochrome P450 reductase. Biochemistry 45, 1421-1434. (Pubitemid 43214807)
    • (2006) Biochemistry , vol.45 , Issue.5 , pp. 1421-1434
    • Grunau, A.1    Paine, M.J.2    Ladbury, J.E.3    Gutierrez, A.4
  • 45
    • 0038650809 scopus 로고    scopus 로고
    • Interflavin electron transfer in human cytochrome P450 reductase is enhanced by coenzyme binding. Relaxation kinetic studies with coenzyme analogues
    • Gutierrez, A., Munro, A. W., Grunau, A., Wolf, C. R., Scrutton, N. S., and Roberts, G. C. (2003) Interflavin electron transfer in human cytochrome P450 reductase is enhanced by coenzyme binding. Relaxation kinetic studies with coenzyme analogues. Eur. J. Biochem. 270, 2612-2621.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2612-2621
    • Gutierrez, A.1    Munro, A.W.2    Grunau, A.3    Wolf, C.R.4    Scrutton, N.S.5    Roberts, G.C.6
  • 47
    • 0037376842 scopus 로고    scopus 로고
    • Electron transfer is activated by calmodulin in the flavin domain of human neuronal nitric oxide synthase
    • DOI 10.1016/S0003-9861(03)00009-2
    • Guan, Z. W., and Iyanagi, T. (2003) Electron transfer is activated by calmodulin in the flavin domain of human neuronal nitric oxide synthase. Arch. Biochem. Biophys. 412, 65-76. (Pubitemid 36324366)
    • (2003) Archives of Biochemistry and Biophysics , vol.412 , Issue.1 , pp. 65-76
    • Guan, Z.-W.1    Iyanagi, T.2
  • 48
    • 0032732706 scopus 로고    scopus 로고
    • Calmodulin activates intramolecular electron transfer between the two flavins of neuronal nitric oxide synthase flavin domain
    • Matsuda, H., and Iyanagi, T. (1999) Calmodulin activates intramolecular electron transfer between the two flavins of neuronal nitric oxide synthase flavin domain. Biochim. Biophys. Acta 1473, 345-355.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 345-355
    • Matsuda, H.1    Iyanagi, T.2
  • 49
    • 0028582164 scopus 로고
    • Calmodulin controls neuronal nitric-oxide synthase by a dual mechanism. Activation of intra- and interdomain electron transfer
    • Abu-Soud, H. M., Yoho, L. L., and Stuehr, D. J. (1994) Calmodulin controls neuronal nitric-oxide synthase by a dual mechanism. Activation of intra- and interdomain electron transfer. J. Biol. Chem. 269, 32047-32050.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32047-32050
    • Abu-Soud, H.M.1    Yoho, L.L.2    Stuehr, D.J.3
  • 50
    • 0032698131 scopus 로고    scopus 로고
    • The 42-amino acid insert in the FMN domain of neuronal nitric-oxide synthase exerts control over Ca(2+)/calmodulin-dependent electron transfer
    • Daff, S., Sagami, I., and Shimizu, T. (1999) The 42-amino acid insert in the FMN domain of neuronal nitric-oxide synthase exerts control over Ca(2+)/calmodulin-dependent electron transfer. J. Biol. Chem. 274, 30589-30595.
    • (1999) J. Biol. Chem. , Issue.274 , pp. 30589-30595
    • Daff, S.1    Sagami, I.2    Shimizu, T.3
  • 51
    • 0035955622 scopus 로고    scopus 로고
    • Rapid Calmodulin-dependent Interdomain Electron Transfer in Neuronal Nitric-oxide Synthase Measured by Pulse Radiolysis
    • DOI 10.1074/jbc.M102537200
    • Kobayashi, K., Tagawa, S., Daff, S., Sagami, I., and Shimizu, T. (2001) Rapid calmodulin-dependent interdomain electron transfer in neuronal nitric-oxide synthase measured by pulse radiolysis. J. Biol. Chem. 276, 39864-39871. (Pubitemid 37391397)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.43 , pp. 39864-39871
    • Kobayashi, K.1    Tagawa, S.2    Daff, S.3    Sagami, I.4    Shimizu, T.5
  • 52
    • 0035968329 scopus 로고    scopus 로고
    • Calmodulin Activates Intersubunit Electron Transfer in the Neuronal Nitric-oxide Synthase Dimer
    • DOI 10.1074/jbc.M100687200
    • Panda, K., Ghosh, S., and Stuehr, D. J. (2001) Calmodulin activates intersubunit electron transfer in the neuronal nitric-oxide synthase dimer. J. Biol. Chem. 276, 23349-23356. (Pubitemid 37410718)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.26 , pp. 23349-23356
    • Panda, K.1    Ghosh, S.2    Stuehr, D.J.3
  • 53
    • 0034703091 scopus 로고    scopus 로고
    • The C termini of constitutive nitric-oxide synthases control electron flow through the flavin and heme domains and affect modulation by calmodulin
    • DOI 10.1074/jbc.M004766200
    • Roman, L. J., Martasek, P., Miller, R. T., Harris, D. E., de La Garza, M. A., Shea, T. M., Kim, J. J., and Masters, B. S. (2000) The C termini of constitutive nitric-oxide synthases control electron flow through the flavin and heme domains and affect modulation by calmodulin. J. Biol. Chem. 275, 29225-29232. (Pubitemid 32043790)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.38 , pp. 29225-29232
    • Roman, L.J.1    Martasek, P.2    Miller, R.T.3    Harris, D.E.4    De La Garza, M.A.5    Shea, T.M.6    Kim, J.-J.P.7    Masters, B.S.S.8
  • 54
    • 34748888339 scopus 로고    scopus 로고
    • Calcium-deficient calmodulin binding and activation of neuronal and inducible nitric oxide synthases
    • DOI 10.1016/j.bbapap.2007.07.019, PII S1570963907001756
    • Spratt, D. E., Taiakina, V., and Guillemette, J. G. (2007) Calcium-deficient calmodulin binding and activation of neuronal and inducible nitric oxide synthases. Biochim. Biophys. Acta 1774, 1351-1358. (Pubitemid 47484293)
    • (2007) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1774 , Issue.10 , pp. 1351-1358
    • Spratt, D.E.1    Taiakina, V.2    Guillemette, J.G.3
  • 57
    • 0042357128 scopus 로고    scopus 로고
    • Nitric-oxide synthase (NOS) reductase domain models suggest a new control element in endothelial NOS that attenuates calmodulin-dependent activity
    • Knudsen, G. M., Nishida, C. R., Mooney, S. D., and Ortiz de Montellano, P. R. (2003) Nitric-oxide synthase (NOS) reductase domain models suggest a new control element in endothelial NOS that attenuates calmodulin-dependent activity. J. Biol. Chem. 278, 31814-31824.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31814-31824
    • Knudsen, G.M.1    Nishida, C.R.2    Mooney, S.D.3    Ortiz De Montellano, P.R.4
  • 58
    • 33646858996 scopus 로고    scopus 로고
    • Intraprotein electron transfer in a two-domain construct of neuronal nitric oxide synthase: The output state in nitric oxide formation
    • DOI 10.1021/bi060223n
    • Feng, C., Tollin, G., Holliday, M. A., Thomas, C., Salerno, J. C., Enemark, J. H., and Ghosh, D. K. (2006) Intraprotein electron transfer in a two-domain construct of neuronal nitric oxide synthase: the output state in nitric oxide formation. Biochemistry 45, 6354-6362. (Pubitemid 43787802)
    • (2006) Biochemistry , vol.45 , Issue.20 , pp. 6354-6362
    • Feng, C.1    Tollin, G.2    Holliday, M.A.3    Thomas, C.4    Salerno, J.C.5    Enemark, J.H.6    Ghosh, D.K.7
  • 59
    • 33646859307 scopus 로고    scopus 로고
    • Nitric-oxide synthase output state. Design and properties of nitric-oxide synthase oxygenase/FMN domain constructs
    • Ghosh, D. K., Holliday, M. A., Thomas, C., Weinberg, J. B., Smith, S. M., and Salerno, J. C. (2006) Nitric-oxide synthase output state. Design and properties of nitric-oxide synthase oxygenase/FMN domain constructs. J. Biol. Chem. 281, 14173-14183.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14173-14183
    • Ghosh, D.K.1    Holliday, M.A.2    Thomas, C.3    Weinberg, J.B.4    Smith, S.M.5    Salerno, J.C.6
  • 60
    • 0141510043 scopus 로고    scopus 로고
    • Distinct influence of N-terminal elements on neuronal nitric-oxide synthase structure and catalysis
    • DOI 10.1074/jbc.M304456200
    • Panda, K., Adak, S., Aulak, K. S., Santolini, J., McDonald, J. F., and Stuehr, D. J. (2003) Distinct influence of N-terminal elements on neuronal nitric-oxide synthase structure and catalysis. J. Biol. Chem. 278, 37122-37131. (Pubitemid 37175226)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37122-37131
    • Panda, K.1    Adak, S.2    Aulak, K.S.3    Santolini, J.4    McDonald, J.F.5    Stuehr, D.J.6
  • 61
    • 33750061297 scopus 로고    scopus 로고
    • Role of Asp(1393) in catalysis, flavin reduction, NADP(H) binding, FAD thermodynamics, and regulation of the nNOS flavoprotein
    • Konas, D. W., Takaya, N., Sharma, M., and Stuehr, D. J. (2006) Role of Asp(1393) in catalysis, flavin reduction, NADP(H) binding, FAD thermodynamics, and regulation of the nNOS flavoprotein. Biochemistry 45, 12596-12609.
    • (2006) Biochemistry , vol.45 , pp. 12596-12609
    • Konas, D.W.1    Takaya, N.2    Sharma, M.3    Stuehr, D.J.4
  • 62
    • 0037197254 scopus 로고    scopus 로고
    • Novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature
    • DOI 10.1002/jcc.10061
    • Tsodikov, O. V., Record, M. T.Jr., and Sergeev, Y. V. (2002) Novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature. J. Comput. Chem. 23, 600-609. (Pubitemid 34312083)
    • (2002) Journal of Computational Chemistry , vol.23 , Issue.6 , pp. 600-609
    • Tsodikov, O.V.1    Thomas Record Jr., M.2    Sergeev, Y.V.3
  • 63
    • 0027223213 scopus 로고
    • Using dysprosium complexes to probe the nitrogenase paramagnetic centers
    • Oliver, M. E., and Hales, B. J. (1993) Using dysprosium complexes to probe the nitrogenase paramagnetic centers. Biochemistry 32, 6058-6064. (Pubitemid 23198766)
    • (1993) Biochemistry , vol.32 , Issue.23 , pp. 6058-6064
    • Oliver, M.E.1    Hales, B.J.2
  • 64
    • 0033578836 scopus 로고    scopus 로고
    • Crucial role of Lys(423) in the electron transfer of neuronal nitricoxide synthase
    • Shimanuki, T., Sato, H., Daff, S., Sagami, I., and Shimizu, T. (1999) Crucial role of Lys(423) in the electron transfer of neuronal nitricoxide synthase. J. Biol. Chem. 274, 26956-26961.
    • (1999) J. Biol. Chem. , Issue.274 , pp. 26956-26961
    • Shimanuki, T.1    Sato, H.2    Daff, S.3    Sagami, I.4    Shimizu, T.5
  • 65
    • 0030585351 scopus 로고    scopus 로고
    • High-level expression of mouse inducible nitric oxide synthase in Escherichia coli requires coexpression with calmodulin
    • DOI 10.1006/bbrc.1996.0763
    • Wu, C., Zhang, J., Abu-Soud, H., Ghosh, D. K., and Stuehr, D. J. (1996) High-level expression of mouse inducible nitric oxide synthase in Escherichia coli requires coexpression with calmodulin. Biochem. Biophys. Res. Commun. 222, 439-444. (Pubitemid 26335035)
    • (1996) Biochemical and Biophysical Research Communications , vol.222 , Issue.2 , pp. 439-444
    • Wu, C.1    Zhang, J.2    Abu-Soud, H.3    Ghosh, D.K.4    Stuehr, D.J.5
  • 67
    • 0032619606 scopus 로고    scopus 로고
    • Fluorescence analysis of flavoproteins
    • Munro, A. W., and Noble, M. A. (1999) Fluorescence analysis of flavoproteins. Methods Mol. Biol. 131, 25-48.
    • (1999) Methods Mol. Biol. , vol.131 , pp. 25-48
    • Munro, A.W.1    Noble, M.A.2
  • 68
    • 0029982073 scopus 로고    scopus 로고
    • EPR spectroscopic characterization of neuronal NO synthase
    • DOI 10.1021/bi9520444
    • Galli, C., MacArthur, R., Abu-Soud, H. M., Clark, P., Stuehr, D. J., and Brudvig, G. W. (1996) EPR spectroscopic characterization of neuronal NO synthase. Biochemistry 35, 2804-2810. (Pubitemid 26099927)
    • (1996) Biochemistry , vol.35 , Issue.8 , pp. 2804-2810
    • Galli, C.1    MacArthur, R.2    Abu-Soud, H.M.3    Clark, P.4    Stuehr, D.J.5    Brudvig, G.W.6
  • 69
    • 0024500293 scopus 로고
    • Location and magnetic relaxation properties of the stable tyrosine radical in photosystem II
    • DOI 10.1021/bi00429a028
    • Innes, J. B., and Brudvig, G. W. (1989) Location and magnetic relaxation properties of the stable tyrosine radical in photosystem II. Biochemistry 28, 1116-1125. (Pubitemid 19058686)
    • (1989) Biochemistry , vol.28 , Issue.3 , pp. 1116-1125
    • Innes, J.B.1    Brudvig, G.W.2
  • 70
    • 33645968442 scopus 로고    scopus 로고
    • NADPH analog binding to constitutive nitric oxide activates electron transfer and NO synthesis
    • Jones, R. J., Gao, Y. T., Simone, T. M., Salerno, J. C., and Smith, S. M. (2006) NADPH analog binding to constitutive nitric oxide activates electron transfer and NO synthesis. Nitric Oxide 14, 228-237.
    • (2006) Nitric Oxide , vol.14 , pp. 228-237
    • Jones, R.J.1    Gao, Y.T.2    Simone, T.M.3    Salerno, J.C.4    Smith, S.M.5
  • 71
    • 0034680319 scopus 로고    scopus 로고
    • Functional interactions in cytochrome P450BM3. Evidence that NADP(H) binding controls redox potentials of the flavin cofactors
    • Murataliev, M. B., and Feyereisen, R. (2000) Functional interactions in cytochrome P450BM3. Evidence that NADP(H) binding controls redox potentials of the flavin cofactors. Biochemistry 39, 12699-12707.
    • (2000) Biochemistry , vol.39 , pp. 12699-12707
    • Murataliev, M.B.1    Feyereisen, R.2
  • 72
    • 24044466133 scopus 로고    scopus 로고
    • Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein
    • DOI 10.1074/jbc.M505562200
    • Toogood, H. S., van Thiel, A., Scrutton, N. S., and Leys, D. (2005) Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein. J. Biol. Chem. 280, 30361-30366. (Pubitemid 41216218)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.34 , pp. 30361-30366
    • Toogood, H.S.1    Van Thiel, A.2    Scrutton, N.S.3    Leys, D.4
  • 74
    • 0142231009 scopus 로고    scopus 로고
    • Mechanism for electron transfer within and between proteins
    • DOI 10.1016/j.cbpa.2003.08.005
    • Page, C. C., Moser, C. C., and Dutton, P. L. (2003) Mechanism for electron transfer within and between proteins. Curr. Opin. Chem. Biol. 7, 551-556. (Pubitemid 37315789)
    • (2003) Current Opinion in Chemical Biology , vol.7 , Issue.5 , pp. 551-556
    • Page, C.C.1    Moser, C.C.2    Dutton, P.L.3
  • 75
    • 0033571222 scopus 로고    scopus 로고
    • N-terminal domain swapping and metal ion binding in nitric oxide synthase dimerization
    • DOI 10.1093/emboj/18.22.6271
    • Crane, B. R., Rosenfeld, R. J., Arvai, A. S., Ghosh, D. K., Ghosh, S., Tainer, J. A., Stuehr, D. J., and Getzoff, E. D. (1999) N-terminal domain swapping and metal ion binding in nitric oxide synthase dimerization. EMBO J. 18, 6271-6281. (Pubitemid 29533231)
    • (1999) EMBO Journal , vol.18 , Issue.22 , pp. 6271-6281
    • Crane, B.R.1    Rosenfeld, R.J.2    Arvai, A.S.3    Ghosh, D.K.4    Ghosh, S.5    Tainer, J.A.6    Stuehr, D.J.7    Getzoff, E.D.8
  • 76
    • 4344566972 scopus 로고    scopus 로고
    • Update on mechanism and catalytic regulation in the NO synthases
    • DOI 10.1074/jbc.R400017200
    • Stuehr, D. J., Santolini, J., Wang, Z. Q., Wei, C. C., and Adak, S. (2004) Update on mechanism and catalytic regulation in the NO synthases. J. Biol. Chem. 279, 36167-36170. (Pubitemid 39128949)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.35 , pp. 36167-36170
    • Stuehr, D.J.1    Santolini, J.2    Wang, Z.-Q.3    Wei, C.-C.4    Adak, S.5
  • 77
    • 0026612806 scopus 로고
    • Ca2+/calmodulin-dependent cytochrome c reductase activity of brain nitric oxide synthase
    • Klatt, P., Heinzel, B., John, M., Kastner, M., Bohme, E., and Mayer, B. (1992) Ca2+/calmodulin-dependent cytochrome c reductase activity of brain nitric oxide synthase. J. Biol. Chem. 267, 11374-11378.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11374-11378
    • Klatt, P.1    Heinzel, B.2    John, M.3    Kastner, M.4    Bohme, E.5    Mayer, B.6
  • 78
    • 0037053289 scopus 로고    scopus 로고
    • Interactions between the isolated oxygenase and reductase domains of neuronal nitric-oxide synthase: Assessing the role of calmodulin
    • Rozhkova, E. A., Fujimoto, N., Sagami, I., Daff, S. N., and Shimizu, T. (2002) Interactions between the isolated oxygenase and reductase domains of neuronal nitric-oxide synthase: assessing the role of calmodulin. J. Biol. Chem. 277, 16888-16894.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16888-16894
    • Rozhkova, E.A.1    Fujimoto, N.2    Sagami, I.3    Daff, S.N.4    Shimizu, T.5
  • 81
    • 33645413839 scopus 로고    scopus 로고
    • Direct measurement by laser flash photolysis of intramolecular electron transfer in a twodomain construct of murine inducible nitric oxide synthase
    • Feng, C., Thomas, C., Holliday, M. A., Tollin, G., Salerno, J. C., Ghosh, D. K., and Enemark, J. H. (2006) Direct measurement by laser flash photolysis of intramolecular electron transfer in a twodomain construct of murine inducible nitric oxide synthase. J. Am. Chem. Soc. 128, 3808-3811.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3808-3811
    • Feng, C.1    Thomas, C.2    Holliday, M.A.3    Tollin, G.4    Salerno, J.C.5    Ghosh, D.K.6    Enemark, J.H.7
  • 83
    • 0038165531 scopus 로고    scopus 로고
    • The binding sites on human heme oxygenase-1 for cytochrome P450 reductase and biliverdin reductase
    • Wang, J., and Ortiz de Montellano, P. R. (2003) The binding sites on human heme oxygenase-1 for cytochrome P450 reductase and biliverdin reductase. J. Biol. Chem. 278, 20069-20076.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20069-20076
    • Wang, J.1    Ortiz De Montellano, P.R.2
  • 84
    • 0030007024 scopus 로고    scopus 로고
    • Endothelial nitric-oxide synthase. Evidence for bidomain structure and successful reconstitution of catalytic activity from two separate domains generated by a baculovirus expression system
    • Chen, P. F., Tsai, A. L., Berka, V., and Wu, K. K. (1996) Endothelial nitric-oxide synthase. Evidence for bidomain structure and successful reconstitution of catalytic activity from two separate domains generated by a baculovirus expression system. J. Biol. Chem. 271, 14631-14635.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14631-14635
    • Chen, P.F.1    Tsai, A.L.2    Berka, V.3    Wu, K.K.4
  • 85
    • 0029160655 scopus 로고
    • Reconstitution of the second step in NO synthesis using the isolated oxygenase and reductase domains of macrophage NO synthase
    • Ghosh, D. K., Abu-Soud, H. M., and Stuehr, D. J. (1995) Reconstitution of the second step in NO synthesis using the isolated oxygenase and reductase domains of macrophage NO synthase. Biochemistry 34, 11316-11320.
    • (1995) Biochemistry , vol.34 , pp. 11316-11320
    • Ghosh, D.K.1    Abu-Soud, H.M.2    Stuehr, D.J.3


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