208 related articles for article (PubMed ID: 23289611)
1. Charge-pairing interactions control the conformational setpoint and motions of the FMN domain in neuronal nitric oxide synthase.
Haque MM; Bayachou M; Fadlalla MA; Durra D; Stuehr DJ
Biochem J; 2013 Mar; 450(3):607-17. PubMed ID: 23289611
[TBL] [Abstract][Full Text] [Related]
2. A kinetic model linking protein conformational motions, interflavin electron transfer and electron flux through a dual-flavin enzyme-simulating the reductase activity of the endothelial and neuronal nitric oxide synthase flavoprotein domains.
Haque MM; Kenney C; Tejero J; Stuehr DJ
FEBS J; 2011 Nov; 278(21):4055-69. PubMed ID: 21848659
[TBL] [Abstract][Full Text] [Related]
3. Distinct conformational behaviors of four mammalian dual-flavin reductases (cytochrome P450 reductase, methionine synthase reductase, neuronal nitric oxide synthase, endothelial nitric oxide synthase) determine their unique catalytic profiles.
Haque MM; Bayachou M; Tejero J; Kenney CT; Pearl NM; Im SC; Waskell L; Stuehr DJ
FEBS J; 2014 Dec; 281(23):5325-40. PubMed ID: 25265015
[TBL] [Abstract][Full Text] [Related]
4. Restricting the conformational freedom of the neuronal nitric-oxide synthase flavoprotein domain reveals impact on electron transfer and catalysis.
Dai Y; Haque MM; Stuehr DJ
J Biol Chem; 2017 Apr; 292(16):6753-6764. PubMed ID: 28232486
[TBL] [Abstract][Full Text] [Related]
5. A cross-domain charge interaction governs the activity of NO synthase.
Haque MM; Tejero J; Bayachou M; Kenney CT; Stuehr DJ
J Biol Chem; 2018 Mar; 293(12):4545-4554. PubMed ID: 29414777
[TBL] [Abstract][Full Text] [Related]
6. Intraprotein electron transfer in a two-domain construct of neuronal nitric oxide synthase: the output state in nitric oxide formation.
Feng C; Tollin G; Holliday MA; Thomas C; Salerno JC; Enemark JH; Ghosh DK
Biochemistry; 2006 May; 45(20):6354-62. PubMed ID: 16700546
[TBL] [Abstract][Full Text] [Related]
7. Heat shock protein 90 enhances the electron transfer between the FMN and heme cofactors in neuronal nitric oxide synthase.
Zheng H; Li J; Feng C
FEBS Lett; 2020 Sep; 594(17):2904-2913. PubMed ID: 32573772
[TBL] [Abstract][Full Text] [Related]
8. Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins.
Ilagan RP; Tiso M; Konas DW; Hemann C; Durra D; Hille R; Stuehr DJ
J Biol Chem; 2008 Jul; 283(28):19603-15. PubMed ID: 18487202
[TBL] [Abstract][Full Text] [Related]
9. Regulation of FMN subdomain interactions and function in neuronal nitric oxide synthase.
Ilagan RP; Tejero J; Aulak KS; Ray SS; Hemann C; Wang ZQ; Gangoda M; Zweier JL; Stuehr DJ
Biochemistry; 2009 May; 48(18):3864-76. PubMed ID: 19290671
[TBL] [Abstract][Full Text] [Related]
10. Interflavin one-electron transfer in the inducible nitric oxide synthase reductase domain and NADPH-cytochrome P450 reductase.
Yamamoto K; Kimura S; Shiro Y; Iyanagi T
Arch Biochem Biophys; 2005 Aug; 440(1):65-78. PubMed ID: 16009330
[TBL] [Abstract][Full Text] [Related]
11. The FAD-shielding residue Phe1395 regulates neuronal nitric-oxide synthase catalysis by controlling NADP+ affinity and a conformational equilibrium within the flavoprotein domain.
Konas DW; Zhu K; Sharma M; Aulak KS; Brudvig GW; Stuehr DJ
J Biol Chem; 2004 Aug; 279(34):35412-25. PubMed ID: 15180983
[TBL] [Abstract][Full Text] [Related]
12. Control of electron transfer and catalysis in neuronal nitric-oxide synthase (nNOS) by a hinge connecting its FMN and FAD-NADPH domains.
Haque MM; Fadlalla MA; Aulak KS; Ghosh A; Durra D; Stuehr DJ
J Biol Chem; 2012 Aug; 287(36):30105-16. PubMed ID: 22722929
[TBL] [Abstract][Full Text] [Related]
13. 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 SG; Poulos TL
J Biol Chem; 2008 Dec; 283(50):34762-72. PubMed ID: 18852262
[TBL] [Abstract][Full Text] [Related]
14. Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module.
Gruez A; Pignol D; Zeghouf M; Covès J; Fontecave M; Ferrer JL; Fontecilla-Camps JC
J Mol Biol; 2000 May; 299(1):199-212. PubMed ID: 10860732
[TBL] [Abstract][Full Text] [Related]
15. C-terminal tail residue Arg1400 enables NADPH to regulate electron transfer in neuronal nitric-oxide synthase.
Tiso M; Konas DW; Panda K; Garcin ED; Sharma M; Getzoff ED; Stuehr DJ
J Biol Chem; 2005 Nov; 280(47):39208-19. PubMed ID: 16150731
[TBL] [Abstract][Full Text] [Related]
16. Role of Asp1393 in catalysis, flavin reduction, NADP(H) binding, FAD thermodynamics, and regulation of the nNOS flavoprotein.
Konas DW; Takaya N; Sharma M; Stuehr DJ
Biochemistry; 2006 Oct; 45(41):12596-609. PubMed ID: 17029414
[TBL] [Abstract][Full Text] [Related]
17. Mechanism of coenzyme binding to human methionine synthase reductase revealed through the crystal structure of the FNR-like module and isothermal titration calorimetry.
Wolthers KR; Lou X; Toogood HS; Leys D; Scrutton NS
Biochemistry; 2007 Oct; 46(42):11833-44. PubMed ID: 17892308
[TBL] [Abstract][Full Text] [Related]
18. Conformation-dependent hydride transfer in neuronal nitric oxide synthase reductase domain.
Welland A; Daff S
FEBS J; 2010 Sep; 277(18):3833-43. PubMed ID: 20718865
[TBL] [Abstract][Full Text] [Related]
19. Crystal structure of the FAD/NADPH-binding domain of rat neuronal nitric-oxide synthase. Comparisons with NADPH-cytochrome P450 oxidoreductase.
Zhang J; Martàsek P; Paschke R; Shea T; Siler Masters BS; Kim JJ
J Biol Chem; 2001 Oct; 276(40):37506-13. PubMed ID: 11473123
[TBL] [Abstract][Full Text] [Related]
20. Relaxation kinetics of cytochrome P450 reductase: internal electron transfer is limited by conformational change and regulated by coenzyme binding.
Gutierrez A; Paine M; Wolf CR; Scrutton NS; Roberts GC
Biochemistry; 2002 Apr; 41(14):4626-37. PubMed ID: 11926825
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]