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Volumn 1814, Issue 12, 2011, Pages 1997-2002

Intraprotein electron transfer between the FMN and heme domains in endothelial nitric oxide synthase holoenzyme

Author keywords

Electron transfer; Kinetics; Mechanism; Nitric oxide synthase

Indexed keywords

CALMODULIN; ENDOTHELIAL NITRIC OXIDE SYNTHASE; FLAVINE MONONUCLEOTIDE; HEME; HOLOENZYME; SEMIQUINONE;

EID: 81755171985     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2011.08.004     Document Type: Article
Times cited : (13)

References (54)
  • 1
    • 0028128416 scopus 로고
    • NO at work
    • DOI 10.1016/0092-8674(94)90267-4
    • H. Schmidt, and U. Walter NO at work Cell 78 1994 919 925 (Pubitemid 24292320)
    • (1994) Cell , vol.78 , Issue.6 , pp. 919-925
    • Schmidt, H.H.H.W.1    Walter, U.2
  • 2
    • 30444439216 scopus 로고    scopus 로고
    • The discovery of nitric oxide and its role in vascular biology
    • S. Moncada, and E.A. Higgs The discovery of nitric oxide and its role in vascular biology Br. J. Pharmacol. 147 2006 S193 S201
    • (2006) Br. J. Pharmacol. , vol.147
    • Moncada, S.1    Higgs, E.A.2
  • 3
    • 33746123934 scopus 로고    scopus 로고
    • Tumors face NO problems?
    • J.R. Lancaster, and K.P. Xie Tumors face NO problems? Cancer Res. 66 2006 6459 6462
    • (2006) Cancer Res. , vol.66 , pp. 6459-6462
    • Lancaster, J.R.1    Xie, K.P.2
  • 4
    • 77957705981 scopus 로고    scopus 로고
    • Potent, highly selective, and orally bioavailable gem-difluorinated monocationic inhibitors of neuronal nitric oxide synthase
    • F. Xue, H. Li, S.L. Delker, J. Fang, P. MartaÍsek, L.J. Roman, T.L. Poulos, and R.B. Silverman Potent, highly selective, and orally bioavailable gem-difluorinated monocationic inhibitors of neuronal nitric oxide synthase J. Am. Chem. Soc. 132 2010 14229 14238
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 14229-14238
    • Xue, F.1    Li, H.2    Delker, S.L.3    Fang, J.4    Martaísek, P.5    Roman, L.J.6    Poulos, T.L.7    Silverman, R.B.8
  • 5
    • 77951040002 scopus 로고    scopus 로고
    • Unexpected binding modes of nitric oxide synthase inhibitors effective in the prevention of a cerebral palsy phenotype in an animal model
    • S.L. Delker, H. Ji, H. Li, J. Jamal, J. Fang, F. Xue, R.B. Silverman, and T.L. Poulos Unexpected binding modes of nitric oxide synthase inhibitors effective in the prevention of a cerebral palsy phenotype in an animal model J. Am. Chem. Soc. 132 2010 5437 5442
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 5437-5442
    • Delker, S.L.1    Ji, H.2    Li, H.3    Jamal, J.4    Fang, J.5    Xue, F.6    Silverman, R.B.7    Poulos, T.L.8
  • 6
    • 65249163408 scopus 로고    scopus 로고
    • Design of selective neuronal nitric oxide synthase inhibitors for the prevention and treatment of neurodegenerative diseases
    • R.B. Silverman Design of selective neuronal nitric oxide synthase inhibitors for the prevention and treatment of neurodegenerative diseases Acc. Chem. Res. 42 2009 439 451
    • (2009) Acc. Chem. Res. , vol.42 , pp. 439-451
    • Silverman, R.B.1
  • 8
    • 70350450411 scopus 로고    scopus 로고
    • Space, time and nitric oxide - Neuronal nitric oxide synthase generates signal pulses
    • J.C. Salerno, and D.K. Ghosh Space, time and nitric oxide - neuronal nitric oxide synthase generates signal pulses FEBS J. 276 2009 6677 6688
    • (2009) FEBS J. , vol.276 , pp. 6677-6688
    • Salerno, J.C.1    Ghosh, D.K.2
  • 10
    • 0036548323 scopus 로고    scopus 로고
    • Intrinsic and extrinsic modulation of nitric oxide synthase activity
    • DOI 10.1021/cr000661e
    • L.J. Roman, P. Martasek, and B.S.S. Masters Intrinsic and extrinsic modulation of nitric oxide synthase activity Chem. Rev. 102 2002 1179 1189 (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
    • 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
    • L.J. Roman, P. Martasek, R.T. Miller, D.E. Harris, M.A. de la Garza, T.M. Shea, J.J.P. Kim, and B.S.S. Masters 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 2000 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
  • 13
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: Structure, function and inhibition
    • DOI 10.1042/0264-6021:3570593
    • W.K. Alderton, C.E. Cooper, and R.G. Knowles Nitric oxide synthases: structure, function and inhibition Biochem. J. 357 2001 593 615 (Pubitemid 32735142)
    • (2001) Biochemical Journal , vol.357 , Issue.3 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 15
    • 0037898947 scopus 로고    scopus 로고
    • Tetrahydrobiopterin radical enzymology
    • C.C. Wei, B.R. Crane, and D.J. Stuehr Tetrahydrobiopterin radical enzymology Chem. Rev. 103 2003 2365 2383
    • (2003) Chem. Rev. , vol.103 , pp. 2365-2383
    • Wei, C.C.1    Crane, B.R.2    Stuehr, D.J.3
  • 16
    • 69249142914 scopus 로고    scopus 로고
    • Regulation of interdomain electron transfer in the NOS output state for NO production
    • C.J. Feng, and G. Tollin Regulation of interdomain electron transfer in the NOS output state for NO production Dalton Trans. 2009 6692 6700
    • (2009) Dalton Trans. , pp. 6692-6700
    • Feng, C.J.1    Tollin, G.2
  • 17
    • 55249112287 scopus 로고    scopus 로고
    • Phosphorylation of endothelial nitric-oxide synthase regulates superoxide generation from the enzyme
    • C.A. Chen, L.J. Druhan, S. Varadharaj, Y.R. Chen, and J.L. Zweier Phosphorylation of endothelial nitric-oxide synthase regulates superoxide generation from the enzyme J. Biol. Chem. 283 2008 27038 27047
    • (2008) J. Biol. Chem. , vol.283 , pp. 27038-27047
    • Chen, C.A.1    Druhan, L.J.2    Varadharaj, S.3    Chen, Y.R.4    Zweier, J.L.5
  • 18
    • 0035968329 scopus 로고    scopus 로고
    • Calmodulin activates intersubunit electron transfer in the neuronal nitric-oxide synthase dimer
    • K. Panda, S. Ghosh, and D.J. Stuehr Calmodulin activates intersubunit electron transfer in the neuronal nitric-oxide synthase dimer J. Biol. Chem. 276 2001 23349 23356
    • (2001) J. Biol. Chem. , vol.276 , pp. 23349-23356
    • Panda, K.1    Ghosh, S.2    Stuehr, D.J.3
  • 19
    • 34247626781 scopus 로고    scopus 로고
    • Conformational and thermodynamic control of electron transfer in neuronal nitric oxide synthase
    • DOI 10.1021/bi7001339
    • A.J. Dunford, S.E.J. Rigby, S. Hay, A.W. Munro, and N.S. Scrutton Conformational and thermodynamic control of electron transfer in neuronal nitric oxide synthase Biochemistry 46 2007 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
  • 23
    • 77956087963 scopus 로고    scopus 로고
    • Pulsed EPR determination of the distance between heme iron and FMN centers in a human inducible nitric oxide synthase
    • A.V. Astashkin, B.O. Elmore, W. Fan, J.G. Guillemette, and C. Feng Pulsed EPR determination of the distance between heme iron and FMN centers in a human inducible nitric oxide synthase J. Am. Chem. Soc. 132 2010 12059 12067
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 12059-12067
    • Astashkin, A.V.1    Elmore, B.O.2    Fan, W.3    Guillemette, J.G.4    Feng, C.5
  • 24
    • 68149166459 scopus 로고    scopus 로고
    • Structural and mechanistic aspects of flavoproteins: Electron transfer through the nitric oxide synthase flavoprotein domain
    • D.J. Stuehr, J. Tejero, and M.M. Haque Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain FEBS J. 276 2009 3959 3974
    • (2009) FEBS J. , vol.276 , pp. 3959-3974
    • Stuehr, D.J.1    Tejero, J.2    Haque, M.M.3
  • 25
    • 33645413839 scopus 로고    scopus 로고
    • Direct measurement by laser flash photolysis of intramolecular electron transfer in a two-domain construct of murine inducible nitric oxide synthase
    • C.J. Feng, C. Thomas, M.A. Holliday, G. Tollin, J.C. Salerno, D.K. Ghosh, and J.H. Enemark Direct measurement by laser flash photolysis of intramolecular electron transfer in a two-domain construct of murine inducible nitric oxide synthase J. Am. Chem. Soc. 128 2006 3808 3811
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3808-3811
    • Feng, C.J.1    Thomas, C.2    Holliday, M.A.3    Tollin, G.4    Salerno, J.C.5    Ghosh, D.K.6    Enemark, J.H.7
  • 26
    • 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
    • C.J. Feng, G. Tollin, M.A. Holliday, C. Thomas, J.C. Salerno, J.H. Enemark, and D.K. Ghosh Intraprotein electron transfer in a two-domain construct of neuronal nitric oxide synthase: the output state in nitric oxide formation Biochemistry 45 2006 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
  • 28
    • 77957769373 scopus 로고    scopus 로고
    • Electron transfer in a human inducible nitric oxide synthase oxygenase/FMN construct co-expressed with the N-terminal globular domain of calmodulin
    • C. Feng, W. Fan, A. Dupont, J. Guy Guillemette, D.K. Ghosh, and G. Tollin Electron transfer in a human inducible nitric oxide synthase oxygenase/FMN construct co-expressed with the N-terminal globular domain of calmodulin FEBS Lett. 584 2010 4335 4338
    • (2010) FEBS Lett. , vol.584 , pp. 4335-4338
    • Feng, C.1    Fan, W.2    Dupont, A.3    Guy Guillemette, J.4    Ghosh, D.K.5    Tollin, G.6
  • 33
    • 0026660191 scopus 로고
    • Spectral characterization of brain and macrophage nitric-oxide synthases - Cytochrome-P-450-like hemeproteins that contain a flavin semiquinone radical
    • D.J. Stuehr, and M. Ikeda-Saito Spectral characterization of brain and macrophage nitric-oxide synthases - cytochrome-P-450-like hemeproteins that contain a flavin semiquinone radical J. Biol. Chem. 267 1992 20547 20550
    • (1992) J. Biol. Chem. , vol.267 , pp. 20547-20550
    • Stuehr, D.J.1    Ikeda-Saito, M.2
  • 34
    • 0037458745 scopus 로고    scopus 로고
    • Redox properties of human endothelial nitric-oxide synthase oxygenase and reductase domains purified from yeast expression system
    • DOI 10.1074/jbc.M209606200
    • M. Du, H.C. Yeh, V. Berka, L.H. Wang, and A.L. Tsai Redox properties of human endothelial nitric-oxide synthase oxygenase and reductase domains purified from yeast expression system J. Biol. Chem. 278 2003 6002 6011 (Pubitemid 36800850)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.8 , pp. 6002-6011
    • Du, M.1    Yeh, H.-C.2    Berka, V.3    Wang, L.-H.4    Tsai, A.-L.5
  • 35
    • 0344240118 scopus 로고    scopus 로고
    • Rapid kinetic studies of electron transfer in the three isoforms of nitric oxide synthase
    • R.T. Miller, P. Martasek, T. Omura, and B.S.S. Masters Rapid kinetic studies of electron transfer in the three isoforms of nitric oxide synthase Biochem. Biophys. Res. Commun. 265 1999 184 188
    • (1999) Biochem. Biophys. Res. Commun. , vol.265 , pp. 184-188
    • Miller, R.T.1    Martasek, P.2    Omura, T.3    Masters, B.S.S.4
  • 37
    • 80051797210 scopus 로고    scopus 로고
    • Effect of solution viscosity on intraprotein electron transfer between the FMN and heme domains in inducible nitric oxide synthase
    • W. Li, W. Fan, B.O. Elmore, and C. Feng Effect of solution viscosity on intraprotein electron transfer between the FMN and heme domains in inducible nitric oxide synthase FEBS Lett. 585 2011 2622 2626
    • (2011) FEBS Lett. , vol.585 , pp. 2622-2626
    • Li, W.1    Fan, W.2    Elmore, B.O.3    Feng, C.4
  • 38
    • 0032489512 scopus 로고    scopus 로고
    • Electron transfer and catalytic activity of nitric oxide synthases. Chimeric constructs of the neuronal, inducible, and endothelial isoforms
    • DOI 10.1074/jbc.273.10.5566
    • C.R. Nishida, and P.R.O. de Montellano Electron transfer and catalytic activity of nitric oxide synthases: chimeric constructs of the neuronal, inducible, and endothelial isoforms J. Biol. Chem. 273 1998 5566 5571 (Pubitemid 28124023)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.10 , pp. 5566-5571
    • Nishida, C.R.1    De Montellano, P.R.O.2
  • 39
    • 0035916295 scopus 로고    scopus 로고
    • Determination of the redox properties of human NADPH-cytochrome P450 reductase
    • DOI 10.1021/bi001718u
    • A.W. Munro, M.A. Noble, L. Robledo, S.N. Daff, and S.K. Chapman Determination of the redox properties of human NADPH-cytochrome P450 reductase Biochemistry 40 2001 1956 1963 (Pubitemid 32165664)
    • (2001) Biochemistry , vol.40 , Issue.7 , pp. 1956-1963
    • Munro, A.W.1    Noble, M.A.2    Robledo, L.3    Daff, S.N.4    Chapman, S.K.5
  • 40
    • 47849091787 scopus 로고    scopus 로고
    • Deletion of the autoregulatory insert modulates intraprotein electron transfer in rat neuronal nitric oxide synthase
    • C.J. Feng, L.J. Roman, J.T. Hazzard, D.K. Ghosh, G. Tollin, and B.S.S. Masters Deletion of the autoregulatory insert modulates intraprotein electron transfer in rat neuronal nitric oxide synthase FEBS Lett. 582 2008 2768 2772
    • (2008) FEBS Lett. , vol.582 , pp. 2768-2772
    • Feng, C.J.1    Roman, L.J.2    Hazzard, J.T.3    Ghosh, D.K.4    Tollin, G.5    Masters, B.S.S.6
  • 41
    • 84955331315 scopus 로고    scopus 로고
    • Interprotein and intraprotein electron transfer mechanisms
    • G. Tollin Interprotein and intraprotein electron transfer mechanisms Electron Transfer Chem. IV 2001 202 231
    • (2001) Electron Transfer Chem. , vol.4 , pp. 202-231
    • Tollin, G.1
  • 42
    • 9944241407 scopus 로고    scopus 로고
    • Electrical circuitry in biology: Emerging principles from protein structure
    • DOI 10.1016/j.sbi.2004.10.002, PII S0959440X04001782
    • D. Leys, and N.S. Scrutton Electrical circuitry in biology: emerging principles from protein structure Curr. Opin. Struct. Biol. 14 2004 642 647 (Pubitemid 39592573)
    • (2004) Current Opinion in Structural Biology , vol.14 , Issue.6 , pp. 642-647
    • Leys, D.1    Scrutton, N.S.2
  • 44
    • 0043154640 scopus 로고    scopus 로고
    • Nitric oxide synthases: Domain structure and alignment in enzyme function and control
    • D.K. Ghosh, and J.C. Salerno Nitric oxide synthases: domain structure and alignment in enzyme function and control Front. Biosci. 8 2003 D193 D209
    • (2003) Front. Biosci. , vol.8
    • Ghosh, D.K.1    Salerno, J.C.2
  • 45
    • 51849113324 scopus 로고    scopus 로고
    • Importance of the domain-domain interface to the catalytic action of the NO synthase reductase domain
    • A. Welland, P.E. Garnaud, M. Kitamura, C.S. Miles, and S. Daff Importance of the domain-domain interface to the catalytic action of the NO synthase reductase domain Biochemistry 47 2008 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
  • 46
    • 77952240774 scopus 로고    scopus 로고
    • NO synthase: Structures and mechanisms
    • S. Daff NO synthase: structures and mechanisms Nitric Oxide 23 2010 1 11
    • (2010) Nitric Oxide , vol.23 , pp. 1-11
    • Daff, S.1
  • 48
    • 0038152781 scopus 로고    scopus 로고
    • Chimeric enzymes of cytochrome P450 oxidoreductase and neuronal nitric-oxide synthase reductase domain reveal structural and functional differences
    • DOI 10.1074/jbc.M212309200
    • L.J. Roman, J. McLain, and B.S.S. Masters Chimeric enzymes of cytochrome P450 oxidoreductase and neuronal nitric-oxide synthase reductase domain reveal structural and functional differences J. Biol. Chem. 278 2003 25700 25707 (Pubitemid 36835325)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.28 , pp. 25700-25707
    • Roman, L.J.1    McLain, J.2    Masters, B.S.S.3
  • 50
    • 77956070332 scopus 로고    scopus 로고
    • Surface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase
    • J. Tejero, L. Hannibal, A. Mustovich, and D.J. Stuehr Surface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase J. Biol. Chem. 285 2010 27232 27240
    • (2010) J. Biol. Chem. , vol.285 , pp. 27232-27240
    • Tejero, J.1    Hannibal, L.2    Mustovich, A.3    Stuehr, D.J.4
  • 52
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • C.C. Page, C.C. Moser, X.X. Chen, and P.L. Dutton Natural engineering principles of electron tunnelling in biological oxidation-reduction Nature 402 1999 47 52
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.X.3    Dutton, P.L.4
  • 54
    • 77954628406 scopus 로고    scopus 로고
    • Nature of the energy landscape for gated electron transfer in a dynamic redox protein
    • S. Hay, S. Brenner, B. Khara, A.M. Quinn, S.E.J. Rigby, and N.S. Scrutton Nature of the energy landscape for gated electron transfer in a dynamic redox protein J. Am. Chem. Soc. 132 2010 9738 9745
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9738-9745
    • Hay, S.1    Brenner, S.2    Khara, B.3    Quinn, A.M.4    Rigby, S.E.J.5    Scrutton, N.S.6


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