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Journal Abstract Search
350 related items for PubMed ID: 7756296
1. X-ray absorption spectroscopic studies of the Fe(II) active site of catechol 2,3-dioxygenase. Implications for the extradiol cleavage mechanism. Shu L, Chiou YM, Orville AM, Miller MA, Lipscomb JD, Que L. Biochemistry; 1995 May 23; 34(20):6649-59. PubMed ID: 7756296 [Abstract] [Full Text] [Related]
2. Models for extradiol cleaving catechol dioxygenases: syntheses, structures, and reactivities of iron(II)-monoanionic catecholate complexes. Jo DH, Chiou YM, Que L. Inorg Chem; 2001 Jun 18; 40(13):3181-90. PubMed ID: 11399191 [Abstract] [Full Text] [Related]
3. 4-nitrocatechol as a probe of a Mn(II)-dependent extradiol-cleaving catechol dioxygenase (MndD): comparison with relevant Fe(II) and Mn(II) model complexes. Reynolds MF, Costas M, Ito M, Jo DH, Tipton AA, Whiting AK, Que L. J Biol Inorg Chem; 2003 Feb 18; 8(3):263-72. PubMed ID: 12589562 [Abstract] [Full Text] [Related]
4. Substrate, substrate analogue, and inhibitor interactions with the ferrous active site of catechol 2,3-dioxygenase monitored through XAS studies. Bertini I, Briganti F, Mangani S, Nolting HF, Scozzafava A. FEBS Lett; 1994 Aug 22; 350(2-3):207-12. PubMed ID: 8070565 [Abstract] [Full Text] [Related]
5. Novel iron(III) complexes of sterically hindered 4N ligands: regioselectivity in biomimetic extradiol cleavage of catechols. Mayilmurugan R, Stoeckli-Evans H, Palaniandavar M. Inorg Chem; 2008 Aug 04; 47(15):6645-58. PubMed ID: 18597419 [Abstract] [Full Text] [Related]
6. Iron(III) complexes of tripodal monophenolate ligands as models for non-heme catechol dioxygenase enzymes: correlation of dioxygenase activity with ligand stereoelectronic properties. Mayilmurugan R, Visvaganesan K, Suresh E, Palaniandavar M. Inorg Chem; 2009 Sep 21; 48(18):8771-83. PubMed ID: 19694480 [Abstract] [Full Text] [Related]
7. Novel iron(III) complexes of tripodal and linear tetradentate bis(phenolate) ligands: close relevance to intradiol-cleaving catechol dioxygenases. Velusamy M, Palaniandavar M, Gopalan RS, Kulkarni GU. Inorg Chem; 2003 Dec 15; 42(25):8283-93. PubMed ID: 14658880 [Abstract] [Full Text] [Related]
8. An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Ppseudomonas putida mt-2. Kita A, Kita S, Fujisawa I, Inaka K, Ishida T, Horiike K, Nozaki M, Miki K. Structure; 1999 Jan 15; 7(1):25-34. PubMed ID: 10368270 [Abstract] [Full Text] [Related]
9. [17O]Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase. Evidence for binding of exogenous ligands to the active site Fe2+ of extradiol dioxygenases. Arciero DM, Orville AM, Lipscomb JD. J Biol Chem; 1985 Nov 15; 260(26):14035-44. PubMed ID: 2997190 [Abstract] [Full Text] [Related]
10. Iron(III) complexes of sterically hindered tetradentate monophenolate ligands as functional models for catechol 1,2-dioxygenases: the role of ligand stereoelectronic properties. Velusamy M, Mayilmurugan R, Palaniandavar M. Inorg Chem; 2004 Oct 04; 43(20):6284-93. PubMed ID: 15446874 [Abstract] [Full Text] [Related]
11. Synthesis, structure, spectra and reactivity of iron(III) complexes of facially coordinating and sterically hindering 3N ligands as models for catechol dioxygenases. Sundaravel K, Dhanalakshmi T, Suresh E, Palaniandavar M. Dalton Trans; 2008 Dec 28; (48):7012-25. PubMed ID: 19050788 [Abstract] [Full Text] [Related]
12. Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase. Kovaleva EG, Lipscomb JD. Biochemistry; 2008 Oct 28; 47(43):11168-70. PubMed ID: 18826259 [Abstract] [Full Text] [Related]
13. Spectroscopic and electronic structure studies of 2,3-dihydroxybiphenyl 1,2-dioxygenase: O2 reactivity of the non-heme ferrous site in extradiol dioxygenases. Davis MI, Wasinger EC, Decker A, Pau MY, Vaillancourt FH, Bolin JT, Eltis LD, Hedman B, Hodgson KO, Solomon EI. J Am Chem Soc; 2003 Sep 17; 125(37):11214-27. PubMed ID: 16220940 [Abstract] [Full Text] [Related]
14. Modeling the 2-His-1-carboxylate facial triad: iron-catecholato complexes as structural and functional models of the extradiol cleaving dioxygenases. Bruijnincx PC, Lutz M, Spek AL, Hagen WR, Weckhuysen BM, van Koten G, Gebbink RJ. J Am Chem Soc; 2007 Feb 28; 129(8):2275-86. PubMed ID: 17266307 [Abstract] [Full Text] [Related]
15. Conversion of extradiol aromatic ring-cleaving homoprotocatechuate 2,3-dioxygenase into an intradiol cleaving enzyme. Groce SL, Lipscomb JD. J Am Chem Soc; 2003 Oct 01; 125(39):11780-1. PubMed ID: 14505375 [Abstract] [Full Text] [Related]