메뉴 건너뛰기




Volumn 584, Issue 20, 2010, Pages 4335-4338

Electron transfer in a human inducible nitric oxide synthase oxygenase/FMN construct co-expressed with the N-terminal globular domain of calmodulin

Author keywords

Calmodulin; Heme FMN electron transfer; Intraprotein kinetics; Laser flash photolysis; Nitric oxide synthase

Indexed keywords

CALMODULIN; EDETIC ACID; FLAVINE MONONUCLEOTIDE; HEME; INDUCIBLE NITRIC OXIDE SYNTHASE;

EID: 77957769373     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.09.028     Document Type: Article
Times cited : (9)

References (35)
  • 1
    • 0028128416 scopus 로고
    • NO at work
    • Schmidt H., Walter U. NO at work. Cell 1994, 78:919-925.
    • (1994) Cell , vol.78 , pp. 919-925
    • Schmidt, H.1    Walter, U.2
  • 2
    • 30444439216 scopus 로고    scopus 로고
    • The discovery of nitric oxide and its role in vascular biology
    • Moncada S., Higgs E.A. The discovery of nitric oxide and its role in vascular biology. Br. J. Pharmacol. 2006, 147:S193-S201.
    • (2006) Br. J. Pharmacol. , vol.147
    • Moncada, S.1    Higgs, E.A.2
  • 3
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: structure, function and inhibition
    • Alderton W.K., Cooper C.E., Knowles R.G. Nitric oxide synthases: structure, function and inhibition. Biochem. J. 2001, 357:593-615.
    • (2001) Biochem. J. , vol.357 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 4
    • 0036548323 scopus 로고    scopus 로고
    • Intrinsic and extrinsic modulation of nitric oxide synthase activity
    • Roman L.J., Martasek P., Masters B.S.S. Intrinsic and extrinsic modulation of nitric oxide synthase activity. Chem. Rev. 2002, 102:1179-1189.
    • (2002) Chem. Rev. , vol.102 , pp. 1179-1189
    • Roman, L.J.1    Martasek, P.2    Masters, B.S.S.3
  • 5
    • 0030715301 scopus 로고    scopus 로고
    • An autoinhibitory control element defines calcium-regulated isoforms of nitric oxide synthase
    • Salerno J.C., et al. An autoinhibitory control element defines calcium-regulated isoforms of nitric oxide synthase. J. Biol. Chem. 1997, 272:29769-29777.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29769-29777
    • Salerno, J.C.1
  • 6
    • 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
    • Roman L.J., Martasek P., Miller R.T., Harris D.E., de la Garza M.A., Shea T.M., Kim J.J.P., Masters B.S.S. 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. 2000, 275:29225-29232.
    • (2000) J. Biol. Chem. , vol.275 , 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
  • 7
    • 69249142914 scopus 로고    scopus 로고
    • Regulation of interdomain electron transfer in the NOS output state for NO production
    • Feng C.J., Tollin G. 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
  • 8
    • 55249112287 scopus 로고    scopus 로고
    • Phosphorylation of endothelial nitric-oxide synthase regulates superoxide generation from the enzyme
    • Chen C.A., Druhan L.J., Varadharaj S., Chen Y.R., Zweier J.L. Phosphorylation of endothelial nitric-oxide synthase regulates superoxide generation from the enzyme. J. Biol. Chem. 2008, 283:27038-27047.
    • (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
  • 9
    • 0035968329 scopus 로고    scopus 로고
    • Calmodulin activates intersubunit electron transfer in the neuronal nitric-oxide synthase dimer
    • Panda K., Ghosh S., Stuehr D.J. Calmodulin activates intersubunit electron transfer in the neuronal nitric-oxide synthase dimer. J. Biol. Chem. 2001, 276:23349-23356.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23349-23356
    • Panda, K.1    Ghosh, S.2    Stuehr, D.J.3
  • 10
    • 34247626781 scopus 로고    scopus 로고
    • Conformational and thermodynamic control of electron transfer in neuronal nitric oxide synthase
    • Dunford A.J., Rigby S.E.J., Hay S., Munro A.W., Scrutton N.S. Conformational and thermodynamic control of electron transfer in neuronal nitric oxide synthase. Biochemistry 2007, 46:5018-5029.
    • (2007) Biochemistry , vol.46 , pp. 5018-5029
    • Dunford, A.J.1    Rigby, S.E.J.2    Hay, S.3    Munro, A.W.4    Scrutton, N.S.5
  • 11
    • 18844474423 scopus 로고    scopus 로고
    • Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase
    • Noble M.A., et al. Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase. Biochemistry 1999, 38:16413-16418.
    • (1999) Biochemistry , vol.38 , pp. 16413-16418
    • Noble, M.A.1
  • 12
    • 2442500558 scopus 로고    scopus 로고
    • Thermodynamics of oxidation-reduction reactions in mammalian nitric-oxide synthase isoforms
    • Gao Y.T., et al. Thermodynamics of oxidation-reduction reactions in mammalian nitric-oxide synthase isoforms. J. Biol. Chem. 2004, 279:18759-18766.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18759-18766
    • Gao, Y.T.1
  • 13
    • 0034949599 scopus 로고    scopus 로고
    • Control of electron transfer in neuronal NO synthase
    • Daff S., et al. Control of electron transfer in neuronal NO synthase. Biochem. Soc. Trans. 2001, 29:147-152.
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 147-152
    • Daff, S.1
  • 14
    • 77956087963 scopus 로고    scopus 로고
    • Pulsed EPR determination of the distance between heme iron and FMN centers in a human inducible nitric oxide synthase
    • Astashkin A.V., Elmore B.O., Fan W., Guillemette J.G., Feng C. Pulsed EPR determination of the distance between heme iron and FMN centers in a human inducible nitric oxide synthase. J. Am. Chem. Soc. 2010, 132:12059-12067.
    • (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
  • 15
    • 68149166459 scopus 로고    scopus 로고
    • Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain
    • Stuehr D.J., Tejero J., Haque M.M. Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain. FEBS J. 2009, 276:3959-3974.
    • (2009) FEBS J. , vol.276 , pp. 3959-3974
    • Stuehr, D.J.1    Tejero, J.2    Haque, M.M.3
  • 16
    • 0043154640 scopus 로고    scopus 로고
    • Nitric oxide synthases: domain structure and alignment in enzyme function and control
    • Ghosh D.K., Salerno J.C. Nitric oxide synthases: domain structure and alignment in enzyme function and control. Front. Biosci. 2003, 8:D193-D209.
    • (2003) Front. Biosci. , vol.8
    • Ghosh, D.K.1    Salerno, J.C.2
  • 17
    • 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
    • Feng C.J., Tollin G., Holliday M.A., Thomas C., Salerno J.C., Enemark J.H., Ghosh D.K. Intraprotein electron transfer in a two-domain construct of neuronal nitric oxide synthase: the output state in nitric oxide formation. Biochemistry 2006, 45:6354-6362.
    • (2006) Biochemistry , vol.45 , pp. 6354-6362
    • Feng, C.J.1    Tollin, G.2    Holliday, M.A.3    Thomas, C.4    Salerno, J.C.5    Enemark, J.H.6    Ghosh, D.K.7
  • 18
    • 57149128450 scopus 로고    scopus 로고
    • Intraprotein electron transfer in inducible nitric oxide synthase holoenzyme
    • Feng C.J., et al. Intraprotein electron transfer in inducible nitric oxide synthase holoenzyme. J. Biol. Inorg. Chem. 2009, 14:133-142.
    • (2009) J. Biol. Inorg. Chem. , vol.14 , pp. 133-142
    • Feng, C.J.1
  • 19
    • 47849091787 scopus 로고    scopus 로고
    • Deletion of the autoregulatory insert modulates intraprotein electron transfer in rat neuronal nitric oxide synthase
    • Feng C.J., Roman L.J., Hazzard J.T., Ghosh D.K., Tollin G., Masters B.S.S. Deletion of the autoregulatory insert modulates intraprotein electron transfer in rat neuronal nitric oxide synthase. FEBS Lett. 2008, 582:2768-2772.
    • (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
  • 20
    • 34247863706 scopus 로고    scopus 로고
    • Direct measurement by laser flash photolysis of intraprotein electron transfer in a rat neuronal nitric oxide synthase
    • Feng C.J., Tollin G., Hazzard J.T., Nahm N.J., Guillemette J.G., Salerno J.C., Ghosh D.K. Direct measurement by laser flash photolysis of intraprotein electron transfer in a rat neuronal nitric oxide synthase. J. Am. Chem. Soc. 2007, 129:5621-5629.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5621-5629
    • Feng, C.J.1    Tollin, G.2    Hazzard, J.T.3    Nahm, N.J.4    Guillemette, J.G.5    Salerno, J.C.6    Ghosh, D.K.7
  • 21
    • 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
    • Feng C.J., Thomas C., Holliday M.A., Tollin G., Salerno J.C., Ghosh D.K., Enemark J.H. 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. 2006, 128:3808-3811.
    • (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
  • 22
    • 66149139413 scopus 로고    scopus 로고
    • Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthase
    • Ilagan R.P., et al. Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthase. Biochemistry 2009, 48:3864-3876.
    • (2009) Biochemistry , vol.48 , pp. 3864-3876
    • Ilagan, R.P.1
  • 23
    • 58049199399 scopus 로고    scopus 로고
    • Exploring the electron transfer properties of neuronal nitric oxide synthase by reversal of the FMN redox potential
    • Li H., Das A., Sibhatu H., Jamal J., Sligar S.G., Poulos T.L. Exploring the electron transfer properties of neuronal nitric oxide synthase by reversal of the FMN redox potential. J. Biol. Chem. 2008, 283:34762-34772.
    • (2008) J. Biol. Chem. , vol.283 , pp. 34762-34772
    • Li, H.1    Das, A.2    Sibhatu, H.3    Jamal, J.4    Sligar, S.G.5    Poulos, T.L.6
  • 24
    • 50349102696 scopus 로고    scopus 로고
    • Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins
    • Ilagan R.P., Tiso M., Konas D.W., Hemann C., Durra D., Hille R., Stuehr D.J. Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins. J. Biol. Chem. 2008, 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
  • 25
    • 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., Daff S. Importance of the domain-domain interface to the catalytic action of the NO synthase reductase domain. Biochemistry 2008, 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
  • 27
    • 77956221747 scopus 로고    scopus 로고
    • A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanism
    • Tejero J., Haque M.M., Durra D., Stuehr D.J. A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanism. J. Biol. Chem. 2010, 285:25941-25949.
    • (2010) J. Biol. Chem. , vol.285 , pp. 25941-25949
    • Tejero, J.1    Haque, M.M.2    Durra, D.3    Stuehr, D.J.4
  • 28
    • 77956070332 scopus 로고    scopus 로고
    • Surface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase
    • Tejero J., Hannibal L., Mustovich A., Stuehr D.J. Surface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase. J. Biol. Chem. 2010, 285:27232-27240.
    • (2010) J. Biol. Chem. , vol.285 , pp. 27232-27240
    • Tejero, J.1    Hannibal, L.2    Mustovich, A.3    Stuehr, D.J.4
  • 29
    • 70149113440 scopus 로고    scopus 로고
    • Mutations in the FMN domain modulate MCD spectra of the heme site in the oxygenase domain of inducible nitric oxide synthase
    • Sempombe J., Elmore B.O., Sun X., Dupont A., Ghosh D.K., Guillemette J.G., Kirk M.L., Feng C. Mutations in the FMN domain modulate MCD spectra of the heme site in the oxygenase domain of inducible nitric oxide synthase. J. Am. Chem. Soc. 2009, 131:6940-6941.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 6940-6941
    • Sempombe, J.1    Elmore, B.O.2    Sun, X.3    Dupont, A.4    Ghosh, D.K.5    Guillemette, J.G.6    Kirk, M.L.7    Feng, C.8
  • 30
    • 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.E., Salerno J.C. Nitric-oxide synthase output state - design and properties of nitric-oxide synthase oxygenase/FMN domain constructs. J. Biol. Chem. 2006, 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.E.5    Salerno, J.C.6
  • 31
    • 33746257423 scopus 로고    scopus 로고
    • Structural studies of constitutive nitric oxide synthases with diatomic ligands bound
    • Li H.Y., Igarashi J., Jamal J., Yang W.P., Poulos T.L. Structural studies of constitutive nitric oxide synthases with diatomic ligands bound. J. Biol. Inorg. Chem. 2006, 11:753-768.
    • (2006) J. Biol. Inorg. Chem. , vol.11 , pp. 753-768
    • Li, H.Y.1    Igarashi, J.2    Jamal, J.3    Yang, W.P.4    Poulos, T.L.5
  • 32
    • 4043170593 scopus 로고    scopus 로고
    • Differential activation of nitric-oxide synthase isozymes by calmodulin-troponin C chimeras
    • Newman E., et al. Differential activation of nitric-oxide synthase isozymes by calmodulin-troponin C chimeras. J. Biol. Chem. 2004, 279:33547-33557.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33547-33557
    • Newman, E.1
  • 33
    • 33646894525 scopus 로고    scopus 로고
    • Binding and activation of nitric oxide synthase isozymes by calmodulin EF hand pairs
    • Spratt D.E., Newman E., Mosher J., Ghosh D.K., Salerno J.C., Guillemette J.G. Binding and activation of nitric oxide synthase isozymes by calmodulin EF hand pairs. FEBS J. 2006, 273:1759-1771.
    • (2006) FEBS J. , vol.273 , pp. 1759-1771
    • Spratt, D.E.1    Newman, E.2    Mosher, J.3    Ghosh, D.K.4    Salerno, J.C.5    Guillemette, J.G.6
  • 34
    • 34447570813 scopus 로고    scopus 로고
    • Differential binding of calmodulin domains to constitutive and inducible nitric oxide synthase enzymes
    • Spratt D.E., Taiakina V., Palmer M., Guillemette J.G. Differential binding of calmodulin domains to constitutive and inducible nitric oxide synthase enzymes. Biochemistry 2007, 46:8288-8300.
    • (2007) Biochemistry , vol.46 , pp. 8288-8300
    • Spratt, D.E.1    Taiakina, V.2    Palmer, M.3    Guillemette, J.G.4
  • 35
    • 0028838821 scopus 로고
    • The calmodulin-nitric oxide synthase interaction - critical role of the calmodulin latch domain in enzyme activation
    • Su Z.Z., Blazing M.A., Fan D., George S.E. The calmodulin-nitric oxide synthase interaction - critical role of the calmodulin latch domain in enzyme activation. J. Biol. Chem. 1995, 270:29117-29122.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29117-29122
    • Su, Z.Z.1    Blazing, M.A.2    Fan, D.3    George, S.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.