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Non-heme iron-dependent dioxygenases : unravelling catalytic mechanisms for complex enzymatic oxidations
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Bugg, Tim and Ramaswamy, S. (2008) Non-heme iron-dependent dioxygenases : unravelling catalytic mechanisms for complex enzymatic oxidations. Current Opinion in Chemical Biology, Vol.12 (No.2). pp. 134-140. ISSN 1367-5931
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Official URL: http://dx.doi.org/10.1016/j.cbpa.2007.12.007
Abstract
The article reviews recent developments in the study of the reaction mechanisms of non-heme iron-dependent dioxygenase enzymes, especially the catechol dioxygenases and arene (Rieske) dioxygenases.
| Item Type: | Journal Item |
|---|---|
| Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology |
| Divisions: | Faculty of Science > Chemistry |
| Library of Congress Subject Headings (LCSH): | Reaction mechanisms (Chemistry), Enzymes, Iron, Oxidation, Metal catalysts |
| Journal or Publication Title: | Current Opinion in Chemical Biology |
| Publisher: | Elsevier Ltd. |
| ISSN: | 1367-5931 |
| Date: | April 2008 |
| Volume: | Vol.12 |
| Number: | No.2 |
| Number of Pages: | 7 |
| Page Range: | pp. 134-140 |
| Identification Number: | 10.1016/j.cbpa.2007.12.007 |
| Status: | Peer Reviewed |
| Publication Status: | Published |
| Access rights to Published version: | Restricted or Subscription Access |
| References: | 1. Bugg TDH: Dioxygenase enzymes: catalytic mechanisms and model chemistry. Tetrahedron 2003, 59:7075-7101. 2. Purpero V, Moran GR: The diverse and pervasive chemistries of the alpha-keto acid dependent enzymes. J Biol Inorg Chem 2007, 12:587-601. 3. �� Kovaleva EG, Lipscomb JD: Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates. Science 2007, 316:453-457. This is a remarkable structure determination of catalytic intermediates in the extradiol dioxygenase mechanism. 4. Winfield CJ, Al-Mahrizy Z, Gravestock M, Bugg TDH: Elucidation of the catalytic mechanisms of the non-haem iron-dependent catechol dioxygenases: synthesism of carba analogues for hydroperoxide reaction intermediates. J Chem Soc Perkin Trans 2000, 1:3277-3289. 5. Bugg TDH, Lin G: Solving the riddle of the intradiol vs. extradiol catechol dioxygenases: how do enzymes control hydroperoxide rearrangements? Chem Commun 2001:941-952. 6. Vaillancourt FH, Bolin JT, Eltis LD: The ins and outs of ringcleaving dioxygenases. Crit Rev Biochem Mol Biol 2006, 41: 241-267. 7. Sugimoto K, Senda T, Aoshima H, Masai E, Fukuda M, Mitsui Y: Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions. Structure 1999, 7:953-965. 8. Mendel S, Arndt A, Bugg TDH: Acid-base catalysis in the extradiol catechol dioxygenase reaction mechanism: sitedirected mutagenesis of His-115 and His-179 in Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB). Biochemistry 2004, 43:13390-13396. 9. Zhang Y, Colabroy KL, Begley TP, Ealick SE: Structural studies on 3-hydroxyanthranilate 3, 4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis. Biochemistry 2005, 44:7632-7643. 10. Sugimoto H, Oda S-I, Otsuki T, Hino T, Yoshida T, Shiro Y: Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase. Proc Natl Acad Sci U S A 2006, 103:2611-2616. 11. Pau MYM, Davis MI, Orville AM, Lipscomb JD, Solomon EI: Spectroscopic and electronic structure study of the enzyme– substrate complex of intradiol dioxygenases: substrate activation by a high-spin ferric non-heme iron site. J Am Chem Soc 2007, 129:1944-1958. 12. Lin G, Reid G, Bugg TDH: Extradiol oxidative cleavage of catechols by ferrous and ferric complexes of 1,4,7- triazacyclononane: insight into the mechanism of the extradiol catechol dioxygenases. J Am Chem Soc 2001, 123:5030-5039. 13. Vaillancourt FH, Barbosa CJ, Spiro TG, Bolin JT, Blades MW, Turner RFB, Eltis LD: Definitive evidence for monoanionic binding of 2,3-dihydroxybiphenyl to 2,3-dihydroxybiphenyl 1,2-dioxygenase from UV resonance Raman spectroscopy, UV/Vis absorption spectroscopy, and crystallography. J Am Chem Soc 2002, 124:2485-2496. 14. Groce SL, Lipscomb JD: Conversion of extradiol aromatic ringcleaving homoprotocatechuate 2,3-dioxygenase into an intradiol cleaving enzyme. J Am Chem Soc 2003, 125:11780- 11781. 15. Schlosrich J, Eley KL, Crowley PJ, Bugg TDH: Directed evolution of a non-heme iron-dependent extradiol catechol dioxygenase: identification of mutants with intradiol oxidative cleavage activity. ChemBiochem 2006, 7:1899-1908. 16. Groce SL, Lipscomb JD: Aromatic ring cleavage by homoprotocatechuate 2,3-dioxygenase: role of His200 in the kinetics of interconversion of reaction cycle intermediates. Biochemistry 2005, 44:7175-7188. 17. Jo D-H, Que L Jr: Tuning the regiospecificity of cleavage in FeIII catecholate complexes: tridentate facial versus meridional ligands. Angew Chem Intl Ed 2000, 39:4284-4287. 18. Bruijnincx PCA, Lutz M, Spek AL, Hagen WR, Weckhuysen BM, van Koten G, Klein Gebbink RJM: Modeling the 2-His-1- carboxylate facial triad: iron-catecholato complexes as structural and functional models of the extradiol cleaving dioxygenases. J Am Chem Soc 2007, 129: 2275-2286. 19. Borowski T, Siegbahn PEM: Mechanism for catechol ring cleavage by non-heme iron intradiol dioxygenases: a hydrid DFT study. J Am Chem Soc 2006, 128:12941-12953. 20. �� Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S: Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron. Science 2003, 299:1039- 1042. In this study a remarkable structure of dioxygen bound side-on to the iron (II) cofactor was obtained by low temperature crystallography. 21. Ferraro DJ, Okerlund AL, Mowers JC, Ramaswamy S: Structural basis for regioselectivity and stereoselectivity of product formation by naphthalene 1,2-dioxygenase. J Bacteriol 2006, 188:6986-6994. 22. � Senda M, Kishigami S, Kimura S, Fukuda M, Ishida T, Senda T: Molecular mechanism of the redox-dependent interaction between NADH dependent ferredoxin reductase and riesketype [2Fe-2S] ferredoxin. J Mol Biol 2007, 373:382-400. This paper describes the detailed structural changes, redox regulation and the complex between reductase and the ferrredoxin components of the Bph oxygenase system. 23. � Ashikawa Y, Fujimoto Z, Noguchi H, Habe H, Omori T, Yamane H, Nojiri H: Electron transfer complex formation between oxygenase and ferredoxin components in Rieske nonheme iron oxygenase system. Structure 2006, 14:1779-1789. This paper captures the electron transport complex between the ferredoxin and a Rieske oxygenase providing details of path of electron transfer. 24. Wolfe MD, Parales JV, Gibson DT, Lipscomb JD: Single turnover chemistry and regulation of O2 activation by the oxygenase component of naphthalene dioxygenase. J Biol Chem 2001, 276:1945-1953. 25. Neibergall MB, Stubna A, Mekmouche Y, Mu¨ nck E, Lipscomb JD: Hydrogen peroxide dependent cis-dihydroxylation of benzoate by fully oxidised benzoate 1,2-dioxygenase. Biochemistry 2007, 46:8004-8016. 26. � Chen K, Que L Jr: Cis-dihydroxylation of olefins by a nonheme iron catalyst: a functional model for the Rieske dioxygenases. Angew Chem Intl Ed 1999, 38:2227-2229. This paper describes the first iron-based model reaction for cis-dihydroxylation. 27. Chen K, Costas M, Kim J, Tipton AK, Que L Jr: Olefin cisdihydroxylation versus epoxidation by non-heme iron catalysts: two faces of an FeIII-OOH coin. J AmChem Soc 2002, 124:3026-3035. 28. � Chakravarty S, Austin RN, Deng D, Groves JT, Lipscomb JD: Radical intermediates in mono-oxygenase reactions of Rieske dioxygenases. J Am Chem Soc 2007, 129:3514-3515. This paper provides clear evidence for the existence of a substrate radical intermediate in the Rieske dioxygenases. 29. Bassan A, Blomberg MRA, Siegbahn PEM: A theoretical study of the cis-dihydroxylation mechanism in naphthalene dioxygenase. J Biol Inorg Chem 2004, 9:439-452. 30. Auldridge ME, McCarty DR, Klee HJ: Plant carotenoid oxygenases and their apocarotenoid products. Curr Opin Plant Biol 2006, 9:315-321. 31. Kloer DP, Ruch S, Al-Babili S, Beyer P, Schulz GE: The structure of a retinal-forming carotenoid oxygenase. Science 2005, 308:267-269. 32. Ye S,Wu X, Wei L, Tang DM, Sun P, Bartlam M, Rao ZH: An insight into the mechanism of human cysteine dioxygenase—key roles of the thioether-bonded tyrosine-cysteine cofactor. J Biol Chem 2007, 282:3391-3402. 33. Galonic DP, Barr EW, Walsh CT, Bollinger JM, Krebs C: Two interconverting Fe (IV) intermediates in aliphatic chlorination by the halogenase CytC3. Nat Chem Biol 2007, 3:113-116. |
| URI: | http://wrap.warwick.ac.uk/id/eprint/30032 |
Data sourced from Thomson Reuters' Web of Knowledge
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