메뉴 건너뛰기




Volumn 110, Issue 38, 2013, Pages

Nitric oxide synthase domain interfaces regulate electron transfer and calmodulin activation

Author keywords

Flavin; Hemoprotein; INOS; NO signaling

Indexed keywords

CALMODULIN; FLAVINE MONONUCLEOTIDE; HEME; NITRIC OXIDE; NITRIC OXIDE SYNTHASE;

EID: 84884294241     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1313331110     Document Type: Article
Times cited : (84)

References (49)
  • 1
    • 84859487532 scopus 로고    scopus 로고
    • Nitric oxide synthases: Regulation and function
    • 837a-837d
    • Förstermann U, Sessa WC (2012) Nitric oxide synthases: Regulation and function. Eur Heart J 33(7):829-837, 837a-837d.
    • (2012) Eur Heart J , vol.33 , Issue.7 , pp. 829-837
    • Förstermann, U.1    Sessa, W.C.2
  • 3
    • 84867121243 scopus 로고    scopus 로고
    • NADPH-cytochrome P450 oxidoreductase: Prototypic member of the diflavin reductase family
    • Iyanagi T, Xia C, Kim J-JP (2012) NADPH-cytochrome P450 oxidoreductase: Prototypic member of the diflavin reductase family. Arch Biochem Biophys 528(1):72-89.
    • (2012) Arch Biochem Biophys , vol.528 , Issue.1 , pp. 72-89
    • Iyanagi, T.1    Xia, C.2    Kim, J.-J.P.3
  • 4
    • 4444354274 scopus 로고    scopus 로고
    • Structural basis for isozyme-specific regulation of electron transfer in nitric-oxide synthase
    • Garcin ED, et al. (2004) Structural basis for isozyme-specific regulation of electron transfer in nitric-oxide synthase. J Biol Chem 279(36):37918-37927.
    • (2004) J Biol Chem , vol.279 , Issue.36 , pp. 37918-37927
    • Garcin, E.D.1
  • 5
    • 80051797210 scopus 로고    scopus 로고
    • Effect of solution viscosity on intraprotein electron transfer between the FMN and heme domains in inducible nitric oxide synthase
    • Li W, Fan W, Elmore BO, Feng C (2011) Effect of solution viscosity on intraprotein electron transfer between the FMN and heme domains in inducible nitric oxide synthase. FEBS Lett 585(16):2622-2626.
    • (2011) FEBS Lett , vol.585 , Issue.16 , pp. 2622-2626
    • Li, W.1    Fan, W.2    Elmore, B.O.3    Feng, C.4
  • 6
    • 0034712677 scopus 로고    scopus 로고
    • Structures of the N(omega)-hydroxy-L-arginine complex of inducible nitric oxide synthase oxygenase dimer with active and inactive pterins
    • Crane BR, et al. (2000) Structures of the N(omega)-hydroxy-L-arginine complex of inducible nitric oxide synthase oxygenase dimer with active and inactive pterins. Biochemistry 39(16):4608-4621.
    • (2000) Biochemistry , vol.39 , Issue.16 , pp. 4608-4621
    • Crane, B.R.1
  • 7
    • 79959898633 scopus 로고    scopus 로고
    • Novel nanomolar imidazo[4,5-b]pyridines as selective nitric oxide synthase (iNOS) inhibitors: SAR and structural insights
    • Grädler U, et al. (2011) Novel nanomolar imidazo[4,5-b]pyridines as selective nitric oxide synthase (iNOS) inhibitors: SAR and structural insights. Bioorg Med Chem Lett 21(14):4228-4232.
    • (2011) Bioorg Med Chem Lett , vol.21 , Issue.14 , pp. 4228-4232
    • Grädler, U.1
  • 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, et al. (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(40):37506-37513.
    • (2001) J Biol Chem , vol.276 , Issue.40 , pp. 37506-37513
    • Zhang, J.1
  • 9
    • 71049135329 scopus 로고    scopus 로고
    • Regulation of interdomain interactions by calmodulin in inducible nitric-oxide synthase
    • Xia C, Misra I, Iyanagi T, Kim J-JP (2009) Regulation of interdomain interactions by calmodulin in inducible nitric-oxide synthase. J Biol Chem 284(44):30708-30717.
    • (2009) J Biol Chem , vol.284 , Issue.44 , pp. 30708-30717
    • Xia, C.1    Misra, I.2    Iyanagi, T.3    Kim, J.-J.P.4
  • 10
    • 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 AV, Elmore BO, Fan W, Guillemette JG, Feng C (2010) Pulsed EPR determination of the distance between heme iron and FMN centers in a human inducible nitric oxide synthase. J Am Chem Soc 132(34):12059-12067.
    • (2010) J Am Chem Soc , vol.132 , Issue.34 , pp. 12059-12067
    • Astashkin, A.V.1    Elmore, B.O.2    Fan, W.3    Guillemette, J.G.4    Feng, C.5
  • 11
    • 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 DJ (2010) Surface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase. J Biol Chem 285(35): 27232-27240.
    • (2010) J Biol Chem , vol.285 , Issue.35 , pp. 27232-27240
    • Tejero, J.1    Hannibal, L.2    Mustovich, A.3    Stuehr, D.J.4
  • 12
    • 77953480345 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry: What is it and what can it tell us?
    • Marcsisin SR, Engen JR (2010) Hydrogen exchange mass spectrometry: What is it and what can it tell us? Anal Bioanal Chem 397(3):967-972.
    • (2010) Anal Bioanal Chem , vol.397 , Issue.3 , pp. 967-972
    • Marcsisin, S.R.1    Engen, J.R.2
  • 13
    • 84876841559 scopus 로고    scopus 로고
    • Higher-order interactions bridge the nitric oxide receptor and catalytic domains of soluble guanylate cyclase
    • Underbakke ES, Iavarone AT, Marletta MA (2013) Higher-order interactions bridge the nitric oxide receptor and catalytic domains of soluble guanylate cyclase. Proc Natl Acad Sci USA 110(17):6777-6782.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.17 , pp. 6777-6782
    • Underbakke, E.S.1    Iavarone, A.T.2    Marletta, M.A.3
  • 14
    • 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, et al. (2006) 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(11):3808-3811.
    • (2006) J Am Chem Soc , vol.128 , Issue.11 , pp. 3808-3811
    • Feng, C.1
  • 17
    • 33846031584 scopus 로고    scopus 로고
    • Surface charge interactions of the FMN module govern catalysis by nitric-oxide synthase
    • Panda K, et al. (2006) Surface charge interactions of the FMN module govern catalysis by nitric-oxide synthase. J Biol Chem 281(48):36819-36827.
    • (2006) J Biol Chem , vol.281 , Issue.48 , pp. 36819-36827
    • Panda, K.1
  • 18
    • 0033578836 scopus 로고    scopus 로고
    • Crucial role of Lys(423) in the electron transfer of neuronal nitric-oxide synthase
    • Shimanuki T, Sato H, Daff S, Sagami I, Shimizu T (1999) Crucial role of Lys(423) in the electron transfer of neuronal nitric-oxide synthase. J Biol Chem 274(38):26956-26961.
    • (1999) J Biol Chem , vol.274 , Issue.38 , pp. 26956-26961
    • Shimanuki, T.1    Sato, H.2    Daff, S.3    Sagami, I.4    Shimizu, T.5
  • 19
    • 4444319291 scopus 로고    scopus 로고
    • Arg410 near the heme proximal ligand of neuronal nitric oxide synthase is critical for both substrate recognition and electron transfer
    • Yadav J, Fujiwara S, Sagami I, Shimizu T (2004) Arg410 near the heme proximal ligand of neuronal nitric oxide synthase is critical for both substrate recognition and electron transfer. Chem Lett 33:752-753.
    • (2004) Chem Lett , vol.33 , pp. 752-753
    • Yadav, J.1    Fujiwara, S.2    Sagami, I.3    Shimizu, T.4
  • 20
    • 0033732759 scopus 로고    scopus 로고
    • Roles of the heme proximal side residues tryptophan409 and tryptophan421 of neuronal nitric oxide synthase in the electron transfer reaction
    • Yumoto T, Sagami I, Daff S, Shimizu T (2000) Roles of the heme proximal side residues tryptophan409 and tryptophan421 of neuronal nitric oxide synthase in the electron transfer reaction. J Inorg Biochem 82(1-4):163-170.
    • (2000) J Inorg Biochem , vol.82 , Issue.1-4 , pp. 163-170
    • Yumoto, T.1    Sagami, I.2    Daff, S.3    Shimizu, T.4
  • 21
    • 67749124524 scopus 로고    scopus 로고
    • Neutralizing a surface charge on the FMN subdomain increases the activity of neuronal nitric-oxide synthase by enhancing the oxygen reactivity of the enzyme heme-nitric oxide complex
    • Haque MM, et al. (2009) Neutralizing a surface charge on the FMN subdomain increases the activity of neuronal nitric-oxide synthase by enhancing the oxygen reactivity of the enzyme heme-nitric oxide complex. J Biol Chem 284(29): 19237-19247.
    • (2009) J Biol Chem , vol.284 , Issue.29 , pp. 19237-19247
    • Haque, M.M.1
  • 22
    • 84860478715 scopus 로고    scopus 로고
    • Structure and dynamics of calmodulin (CaM) bound to nitric oxide synthase peptides: Effects of a phosphomimetic CaM mutation
    • Piazza M, Futrega K, Spratt DE, Dieckmann T, Guillemette JG (2012) Structure and dynamics of calmodulin (CaM) bound to nitric oxide synthase peptides: Effects of a phosphomimetic CaM mutation. Biochemistry 51(17):3651-3661.
    • (2012) Biochemistry , vol.51 , Issue.17 , pp. 3651-3661
    • Piazza, M.1    Futrega, K.2    Spratt, D.E.3    Dieckmann, T.4    Guillemette, J.G.5
  • 23
    • 66149139413 scopus 로고    scopus 로고
    • Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthase
    • Ilagan RP, et al. (2009) Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthase. Biochemistry 48(18):3864-3876.
    • (2009) Biochemistry , vol.48 , Issue.18 , pp. 3864-3876
    • Ilagan, R.P.1
  • 24
    • 84859097238 scopus 로고    scopus 로고
    • FMN fluorescence in inducible NOS constructs reveals a series of conformational states involved in the reductase catalytic cycle
    • Ghosh DK, Ray K, Rogers AJ, Nahm NJ, Salerno JC (2012) FMN fluorescence in inducible NOS constructs reveals a series of conformational states involved in the reductase catalytic cycle. FEBS J 279(7):1306-1317.
    • (2012) FEBS J , vol.279 , Issue.7 , pp. 1306-1317
    • Ghosh, D.K.1    Ray, K.2    Rogers, A.J.3    Nahm, N.J.4    Salerno, J.C.5
  • 25
    • 78650905964 scopus 로고    scopus 로고
    • ROSETTA3: An object-oriented software suite for the simulation and design of macromolecules
    • Leaver-Fay A, et al. (2011) ROSETTA3: An object-oriented software suite for the simulation and design of macromolecules. Methods Enzymol 487:545-574.
    • (2011) Methods Enzymol , vol.487 , pp. 545-574
    • Leaver-Fay, A.1
  • 26
    • 48449094112 scopus 로고    scopus 로고
    • Conformer selection and induced fit in flexible backbone protein-protein docking using computational and NMR ensembles
    • Chaudhury S, Gray JJ (2008) Conformer selection and induced fit in flexible backbone protein-protein docking using computational and NMR ensembles. J Mol Biol 381(4): 1068-1087.
    • (2008) J Mol Biol , vol.381 , Issue.4 , pp. 1068-1087
    • Chaudhury, S.1    Gray, J.J.2
  • 27
    • 80051576392 scopus 로고    scopus 로고
    • KFC2: A knowledge-based hot spot prediction method based on interface solvation, atomic density, and plasticity features
    • Zhu X, Mitchell JC (2011) KFC2: A knowledge-based hot spot prediction method based on interface solvation, atomic density, and plasticity features. Proteins 79(9): 2671-2683.
    • (2011) Proteins , vol.79 , Issue.9 , pp. 2671-2683
    • Zhu, X.1    Mitchell, J.C.2
  • 28
    • 0032533679 scopus 로고    scopus 로고
    • The reductase domain of the human inducible nitric oxide synthase is fully active in the absence of bound calmodulin
    • Newton DC, Montgomery HJ, Guillemette JG (1998) The reductase domain of the human inducible nitric oxide synthase is fully active in the absence of bound calmodulin. Arch Biochem Biophys 359(2):249-257.
    • (1998) Arch Biochem Biophys , vol.359 , Issue.2 , pp. 249-257
    • Newton, D.C.1    Montgomery, H.J.2    Guillemette, J.G.3
  • 29
    • 0029786411 scopus 로고    scopus 로고
    • Characterization of the reductase domain of rat neuronal nitric oxide synthase generated in the methylotrophic yeast Pichia pastoris
    • Gachhui R, et al. (1996) Characterization of the reductase domain of rat neuronal nitric oxide synthase generated in the methylotrophic yeast Pichia pastoris. Calmodulin response is complete within the reductase domain itself. J Biol Chem 271 (34):20594-20602.
    • (1996) Calmodulin Response Is Complete Within the Reductase Domain Itself. J Biol Chem , vol.271 , Issue.34 , pp. 20594-20602
    • Gachhui, R.1
  • 30
    • 0034681382 scopus 로고    scopus 로고
    • Removal of a putative inhibitory element reduces the calcium-dependent calmodulin activation of neuronal nitricoxide synthase
    • Montgomery HJ, Romanov V, Guillemette JG (2000) Removal of a putative inhibitory element reduces the calcium-dependent calmodulin activation of neuronal nitricoxide synthase. J Biol Chem 275(7):5052-5058.
    • (2000) J Biol Chem , vol.275 , Issue.7 , pp. 5052-5058
    • Montgomery, H.J.1    Romanov, V.2    Guillemette, J.G.3
  • 31
    • 0029891615 scopus 로고    scopus 로고
    • High reductase activity of recombinant NOS2 flavoprotein domain lacking the calmodulin binding regulatory sequence
    • Rafferty S, Malech HL (1996) High reductase activity of recombinant NOS2 flavoprotein domain lacking the calmodulin binding regulatory sequence. Biochem Biophys Res Commun 220(3):1002-1007.
    • (1996) Biochem Biophys Res Commun , vol.220 , Issue.3 , pp. 1002-1007
    • Rafferty, S.1    Malech, H.L.2
  • 32
    • 84872912958 scopus 로고    scopus 로고
    • Calmodulin-induced structural changes in endothelial nitric oxide synthase
    • Persechini A, Tran Q-K, Black DJ, Gogol EP (2013) Calmodulin-induced structural changes in endothelial nitric oxide synthase. FEBS Lett 587(3):297-301.
    • (2013) FEBS Lett , vol.587 , Issue.3 , pp. 297-301
    • Persechini, A.1    Tran, Q.-K.2    Black, D.J.3    Gogol, E.P.4
  • 33
    • 77956221747 scopus 로고    scopus 로고
    • A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanism
    • Tejero J, Haque MM, Durra D, Stuehr DJ (2010) A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanism. J Biol Chem 285 (34):25941-25949.
    • (2010) J Biol Chem , vol.285 , Issue.34 , pp. 25941-25949
    • Tejero, J.1    Haque, M.M.2    Durra, D.3    Stuehr, D.J.4
  • 34
    • 45549085992 scopus 로고    scopus 로고
    • Catalytic reduction of a tetrahydrobiopterin radical within nitricoxide synthase
    • Wei C-C, et al. (2008) Catalytic reduction of a tetrahydrobiopterin radical within nitricoxide synthase. J Biol Chem 283(17):11734-11742.
    • (2008) J Biol Chem , vol.283 , Issue.17 , pp. 11734-11742
    • Wei, C.-C.1
  • 35
    • 0032125851 scopus 로고    scopus 로고
    • The high-potential flavin and heme of nitric oxide synthase are not magnetically linked: Implications for electron transfer
    • Perry JM, Moon N, Zhao Y, Dunham WR, Marletta MA (1998) The high-potential flavin and heme of nitric oxide synthase are not magnetically linked: Implications for electron transfer. Chem Biol 5(7):355-364.
    • (1998) Chem Biol , vol.5 , Issue.7 , pp. 355-364
    • Perry, J.M.1    Moon, N.2    Zhao, Y.3    Dunham, W.R.4    Marletta, M.A.5
  • 36
    • 77954762503 scopus 로고    scopus 로고
    • Electron flow through metalloproteins
    • Gray HB, Winkler JR (2010) Electron flow through metalloproteins. Biochim Biophys Acta 1797(9):1563-1572.
    • (2010) Biochim Biophys Acta , vol.1797 , Issue.9 , pp. 1563-1572
    • Gray, H.B.1    Winkler, J.R.2
  • 37
    • 0030723329 scopus 로고    scopus 로고
    • The structure of nitric oxide synthase oxygenase domain and inhibitor complexes
    • Crane BR, et al. (1997) The structure of nitric oxide synthase oxygenase domain and inhibitor complexes. Science 278(5337):425-431.
    • (1997) Science , vol.278 , Issue.5337 , pp. 425-431
    • Crane, B.R.1
  • 38
    • 0032571411 scopus 로고    scopus 로고
    • Structure of nitric oxide synthase oxygenase dimer with pterin and substrate
    • Crane BR, et al. (1998) Structure of nitric oxide synthase oxygenase dimer with pterin and substrate. Science 279(5359):2121-2126.
    • (1998) Science , vol.279 , Issue.5359 , pp. 2121-2126
    • Crane, B.R.1
  • 39
    • 70349496207 scopus 로고    scopus 로고
    • NO formation by a catalytically self-sufficient bacterial nitric oxide synthase from Sorangium cellulosum
    • Agapie T, et al. (2009) NO formation by a catalytically self-sufficient bacterial nitric oxide synthase from Sorangium cellulosum. Proc Natl Acad Sci USA 106(38): 16221-16226.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.38 , pp. 16221-16226
    • Agapie, T.1
  • 40
    • 0028931726 scopus 로고
    • Prokaryotic expression of the heme-and flavinbinding domains of rat neuronal nitric oxide synthase as distinct polypeptides: Identification of the heme-binding proximal thiolate ligand as cysteine-415
    • McMillan K, Masters BSS (1995) Prokaryotic expression of the heme-and flavinbinding domains of rat neuronal nitric oxide synthase as distinct polypeptides: Identification of the heme-binding proximal thiolate ligand as cysteine-415. Biochemistry 34(11):3686-3693.
    • (1995) Biochemistry , vol.34 , Issue.11 , pp. 3686-3693
    • McMillan, K.1    Masters, B.S.S.2
  • 41
    • 0030048595 scopus 로고    scopus 로고
    • Expression of human inducible nitric oxide synthase in Escherichia coli
    • Fossetta JD, et al. (1996) Expression of human inducible nitric oxide synthase in Escherichia coli. FEBS Lett 379(2):135-138.
    • (1996) FEBS Lett , vol.379 , Issue.2 , pp. 135-138
    • Fossetta, J.D.1
  • 42
    • 15444379675 scopus 로고    scopus 로고
    • S-Nitrosation and regulation of inducible nitric oxide synthase
    • Mitchell DA, Erwin PA, Michel T, Marletta MA (2005) S-Nitrosation and regulation of inducible nitric oxide synthase. Biochemistry 44(12):4636-4647.
    • (2005) Biochemistry , vol.44 , Issue.12 , pp. 4636-4647
    • Mitchell, D.A.1    Erwin, P.A.2    Michel, T.3    Marletta, M.A.4
  • 43
    • 0032480754 scopus 로고    scopus 로고
    • Reactions catalyzed by tetrahydrobiopterin-free nitric oxide synthase
    • Rusche KM, Spiering MM, Marletta MA (1998) Reactions catalyzed by tetrahydrobiopterin-free nitric oxide synthase. Biochemistry 37(44):15503-15512.
    • (1998) Biochemistry , vol.37 , Issue.44 , pp. 15503-15512
    • Rusche, K.M.1    Spiering, M.M.2    Marletta, M.A.3
  • 44
    • 33751337111 scopus 로고    scopus 로고
    • Semi-automated data processing of hydrogen exchange mass spectra using HX-Express
    • Weis DD, Engen JR, Kass IJ (2006) Semi-automated data processing of hydrogen exchange mass spectra using HX-Express. J Am Soc Mass Spectrom 17(12):1700-1703.
    • (2006) J Am Soc Mass Spectrom , vol.17 , Issue.12 , pp. 1700-1703
    • Weis, D.D.1    Engen, J.R.2    Kass, I.J.3
  • 46
    • 80052334922 scopus 로고    scopus 로고
    • RosettaRemodel: A generalized framework for flexible backbone protein design
    • Huang P-S, et al. (2011) RosettaRemodel: A generalized framework for flexible backbone protein design. PLoS ONE 6(8):e24109.
    • (2011) PLoS ONE , vol.6 , Issue.8
    • Huang, P.-S.1
  • 47
    • 0038161052 scopus 로고    scopus 로고
    • Protein-protein docking with simultaneous optimization of rigidbody displacement and side-chain conformations
    • Gray JJ, et al. (2003) Protein-protein docking with simultaneous optimization of rigidbody displacement and side-chain conformations. J Mol Biol 331(1):281-299.
    • (2003) J Mol Biol , vol.331 , Issue.1 , pp. 281-299
    • Gray, J.J.1
  • 48
    • 84862572941 scopus 로고    scopus 로고
    • Structural informatics, modeling, and design with an opensource Molecular Software Library (MSL)
    • Kulp DW, et al. (2012) Structural informatics, modeling, and design with an opensource Molecular Software Library (MSL). J Comput Chem 33(20):1645-1661.
    • (2012) J Comput Chem , vol.33 , Issue.20 , pp. 1645-1661
    • Kulp, D.W.1
  • 49
    • 0001765146 scopus 로고
    • An efficient algorithm for a complete link method
    • Defays D (1977) An efficient algorithm for a complete link method. Comput J 20: 364-366.
    • (1977) Comput J , vol.20 , pp. 364-366
    • Defays, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.