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152 related items for PubMed ID: 2334706
1. Spectroscopic and equilibrium studies of ligand and organic substrate binding to indolamine 2,3-dioxygenase. Sono M. Biochemistry; 1990 Feb 13; 29(6):1451-60. PubMed ID: 2334706 [Abstract] [Full Text] [Related]
2. Enzyme kinetic and spectroscopic studies of inhibitor and effector interactions with indoleamine 2,3-dioxygenase. 1. Norharman and 4-phenylimidazole binding to the enzyme as inhibitors and heme ligands. Sono M, Cady SG. Biochemistry; 1989 Jun 27; 28(13):5392-9. PubMed ID: 2789076 [Abstract] [Full Text] [Related]
7. Assignment of the heme axial ligand(s) for the ferric myoglobin (H93G) and heme oxygenase (H25A) cavity mutants as oxygen donors using magnetic circular dichroism. Pond AE, Roach MP, Sono M, Rux AH, Franzen S, Hu R, Thomas MR, Wilks A, Dou Y, Ikeda-Saito M, Ortiz de Montellano PR, Woodruff WH, Boxer SG, Dawson JH. Biochemistry; 1999 Jun 08; 38(23):7601-8. PubMed ID: 10360958 [Abstract] [Full Text] [Related]
8. Nuclear magnetic resonance studies of high-spin ferric hemoproteins. Morishmima I, Ogawa S, Inubushi T, Iizuka T. Adv Biophys; 1978 Jun 08; 11():217-45. PubMed ID: 27954 [Abstract] [Full Text] [Related]
10. Magnetic circular dichroism studies of the active site heme coordination sphere of exogenous ligand-free ferric cytochrome c peroxidase from yeast: effects of sample history and pH. Pond AE, Sono M, Elenkova EA, McRee DE, Goodin DB, English AM, Dawson JH. J Inorg Biochem; 1999 Sep 30; 76(3-4):165-74. PubMed ID: 10605835 [Abstract] [Full Text] [Related]
11. 1-Methyl-DL-tryptophan, beta-(3-benzofuranyl)-DL-alanine (the oxygen analog of tryptophan), and beta-[3-benzo(b)thienyl]-DL-alanine (the sulfur analog of tryptophan) are competitive inhibitors for indoleamine 2,3-dioxygenase. Cady SG, Sono M. Arch Biochem Biophys; 1991 Dec 30; 291(2):326-33. PubMed ID: 1952947 [Abstract] [Full Text] [Related]
12. Magnetic and natural circular dichroism of L-tryptophan 2,3-dioxygenases and indoleamine 2,3-dioxygenase. I. Spectra of ferric and ferrous high spin forms. Uchida K, Shimizu T, Makino R, Sakaguchi K, Iizuka T, Ishimura Y, Nozawa T, Hatano M. J Biol Chem; 1983 Feb 25; 258(4):2519-25. PubMed ID: 6600455 [Abstract] [Full Text] [Related]
13. 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 02; 285(27):21126-33. PubMed ID: 20421301 [Abstract] [Full Text] [Related]
16. The heme environment of recombinant human indoleamine 2,3-dioxygenase. Structural properties and substrate-ligand interactions. Terentis AC, Thomas SR, Takikawa O, Littlejohn TK, Truscott RJ, Armstrong RS, Yeh SR, Stocker R. J Biol Chem; 2002 May 03; 277(18):15788-94. PubMed ID: 11867636 [Abstract] [Full Text] [Related]
17. Effects of formylation of vinyl side chains of heme on optical and ligand binding properties of horse heart ferric myoglobin. Sono M, Asakura T. J Biol Chem; 1976 May 10; 251(9):2664-70. PubMed ID: 4456 [Abstract] [Full Text] [Related]
18. Initial O₂ Insertion Step of the Tryptophan Dioxygenase Reaction Proposed by a Heme-Modification Study. Makino R, Obayashi E, Hori H, Iizuka T, Mashima K, Shiro Y, Ishimura Y. Biochemistry; 2015 Jun 16; 54(23):3604-16. PubMed ID: 25996254 [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 22; 47(16):4752-60. PubMed ID: 18370401 [Abstract] [Full Text] [Related]