153 related articles for article (PubMed ID: 178384)
1. Tryptophan 2,3-dioxygenase: a review of the roles of the heme and copper cofactors in catalysis.
Brady FO
Bioinorg Chem; 1975; 5(2):167-82. PubMed ID: 178384
[TBL] [Abstract][Full Text] [Related]
2. The oxygenated complexes of the two catalytically active oxidation-reduction states of L-tryptophan-2,3-dioxygenase.
Brady FO; Feigelson P
J Biol Chem; 1975 Jul; 250(13):5041-8. PubMed ID: 1150654
[TBL] [Abstract][Full Text] [Related]
3. Radiocopper in L-tryptophan 2,3-dioxygenase isolated from Pseudomonas acidovorans grown in the presence of 64Cu (II).
Brady FO
J Biol Chem; 1975 Jan; 250(1):344-7. PubMed ID: 49351
[TBL] [Abstract][Full Text] [Related]
4. Studies of the copper and heme cofactors of pseudomonad L-tryptophan-2,3-dioxygenase by electron paramagnetic resonance spectroscopy.
Brady FO; Feigelson P; Rajagopalan KV
Arch Biochem Biophys; 1973 Jul; 157(1):63-72. PubMed ID: 4352058
[No Abstract] [Full Text] [Related]
5. On the prosthetic groups of L-tryptophan 2,3-dioxygenase from Pseudomonas: evidence for noninvolvement of copper in the reaction.
Ishimura Y; Hayaishi O
Adv Exp Med Biol; 1976; 74():363-73. PubMed ID: 183474
[TBL] [Abstract][Full Text] [Related]
6. Infrared spectra of carbon monoxide complexes of indoleamine 2,3-dioxygenase and L-tryptophan 2,3-dioxygenases. Effects of substrates on the CO-stretching frequencies.
Uchida K; Bandow H; Makino R; Sakaguchi K; Iizuka T; Ishimura Y
J Biol Chem; 1985 Feb; 260(3):1400-6. PubMed ID: 3871436
[TBL] [Abstract][Full Text] [Related]
7. The ternary complex of PrnB (the second enzyme in the pyrrolnitrin biosynthesis pathway), tryptophan, and cyanide yields new mechanistic insights into the indolamine dioxygenase superfamily.
Zhu X; van Pée KH; Naismith JH
J Biol Chem; 2010 Jul; 285(27):21126-33. PubMed ID: 20421301
[TBL] [Abstract][Full Text] [Related]
8. Negligible amount of copper in hepatic L-tryptophan 2,3-dioxygenase.
Makino R; Ishimura Y
J Biol Chem; 1976 Dec; 251(23):7722-5. PubMed ID: 1002710
[TBL] [Abstract][Full Text] [Related]
9. Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase.
Forouhar F; Anderson JL; Mowat CG; Vorobiev SM; Hussain A; Abashidze M; Bruckmann C; Thackray SJ; Seetharaman J; Tucker T; Xiao R; Ma LC; Zhao L; Acton TB; Montelione GT; Chapman SK; Tong L
Proc Natl Acad Sci U S A; 2007 Jan; 104(2):473-8. PubMed ID: 17197414
[TBL] [Abstract][Full Text] [Related]
10. Asp274 and his346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase.
Littlejohn TK; Takikawa O; Truscott RJ; Walker MJ
J Biol Chem; 2003 Aug; 278(32):29525-31. PubMed ID: 12766158
[TBL] [Abstract][Full Text] [Related]
11. Copper is not essential for the catalytic activity of L-tryptophan 2,3-dioxygenase.
Ishimura Y; Makino R; Ueno R; Sakaguchi K; Brady FO; Feigelson P; Aisen P; Hayaishi O
J Biol Chem; 1980 May; 255(9):3835-7. PubMed ID: 7372650
[No Abstract] [Full Text] [Related]
12. The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase.
Chauhan N; Basran J; Efimov I; Svistunenko DA; Seward HE; Moody PC; Raven EL
Biochemistry; 2008 Apr; 47(16):4761-9. PubMed ID: 18370410
[TBL] [Abstract][Full Text] [Related]
13. Studies on the roles of the catalytic and allosteric sites in modulating the reactivity of tryptophan oxygenase with heme ligands. I. Cyanide derivatives.
Koike K; Feigelson P
Biochemistry; 1971 Aug; 10(18):3378-84. PubMed ID: 4330263
[No Abstract] [Full Text] [Related]
14. On the role of copper in activation of and catalysis by tryptophan-2,3-dioxygenase.
Brady FO; Monaco ME; Forman HJ; Schutz G; Feigelson P
J Biol Chem; 1972 Dec; 247(24):7915-22. PubMed ID: 4640930
[No Abstract] [Full Text] [Related]
15. Analysis of Reaction Intermediates in Tryptophan 2,3-Dioxygenase: A Comparison with Indoleamine 2,3-Dioxygenase.
Basran J; Booth ES; Lee M; Handa S; Raven EL
Biochemistry; 2016 Dec; 55(49):6743-6750. PubMed ID: 27951658
[TBL] [Abstract][Full Text] [Related]
16. Studies on the catalytic and allosteric sites in modulating the reactivity of tryptophan oxygenase with heme ligands. II. Carbon monoxide derivatives.
Koike K; Feigelson P
Biochemistry; 1971 Aug; 10(18):3385-90. PubMed ID: 5118621
[No Abstract] [Full Text] [Related]
17. Stereospecificity of hepatic L-tryptophan 2,3-dioxygenase.
Watanabe Y; Fujiwara M; Yoshida R; Hayaishi O
Biochem J; 1980 Sep; 189(3):393-405. PubMed ID: 6783035
[TBL] [Abstract][Full Text] [Related]
18. pH dependence of the cooperative interactions and conformation of tryptophan oxygenase.
Colman PD; Blanchet SP; Chow E; Feigelson P
J Biol Chem; 1975 Aug; 250(16):6208-13. PubMed ID: 239940
[TBL] [Abstract][Full Text] [Related]
19. A kinetic, spectroscopic, and redox study of human tryptophan 2,3-dioxygenase.
Basran J; Rafice SA; Chauhan N; Efimov I; Cheesman MR; Ghamsari L; Raven EL
Biochemistry; 2008 Apr; 47(16):4752-60. PubMed ID: 18370401
[TBL] [Abstract][Full Text] [Related]
20. How is the distal pocket of a heme protein optimized for binding of tryptophan?
Chauhan N; Basran J; Rafice SA; Efimov I; Millett ES; Mowat CG; Moody PC; Handa S; Raven EL
FEBS J; 2012 Dec; 279(24):4501-9. PubMed ID: 23083473
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]