Oxygen atom transfer into C-H bond in biological and model chemical systems. Mechanistic aspects

Accounts of Chemical Research

Volumn 32, Issue 9, 1999, Pages 763-771

  Shilov, Alexander E ^a   Shteinman, Albert A ^a  

^a INSTITUTE OF PROBLEMS OF CHEMICAL PHYSICS   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

ALKANE; CARBON; CARBOXYLIC ACID; CYTOCHROME P450; HEME DERIVATIVE; HYDROGEN; IRON COMPLEX; METALLOPORPHYRIN; METHANE; ORGANIC COMPOUND; OXYGEN; RHODIUM COMPLEX; ZINC;

ARTICLE; CHEMICAL REACTION; CHEMICAL STRUCTURE; COMPLEX FORMATION; HYDROGEN BOND; HYDROXYLATION; OXIDATION;

EID: 0032818413     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar980009u     Document Type: Article

References (61)

1. (a) Shilov, A. E. Metal Complexes in Biomimetic Chemical Reactions; CRC Press: New York, 1997.
2. (b) Karasevich, E. I.; Kulikova V. S.; Shilov, A. E.; Shteinman, A. A. Biomimetic alkane oxidation involving metal complexes. Russ. Chem. Rev. 1998, 67, 335-355.
3. (c) Shteinman, A. A. Oxygen transfer catalysis by chemical analogs of monooxygenases. Russ. Chem. Bull. 1993, 42, 227-234.
4. (a) Valentine, J. S., Foote, C. S., Greenberg, A., Liebman, J. F., Eds. Active Oxygen in Biochemistry, Chapmen and Hall: London, 1995.
5. (b) Sheldon, R. A.; Kochi, J. K. Metal-Catalyzed Oxidations of Organic Compounds; Academic Press: New York, 1981.
6. (c) Meunier, B. Metalloporphyrins as Versatile Catalysts for Oxidation Reactions and Oxidative DNA Cleavage, Chem. Rev. 1992, 92, 1411-1456.
7. (a) Shilov, A. E.; Shteinman, A. A. Activation of Saturated Hydrocarbons by Metal Complexes in Solution. Coord. Chem. Rev. 1977, 24, 97-143.
8. (b) Shilov, A. E.; Shul'pin, G. B. Activation of C-H Bonds by Metal Complexes. Chem. Rev. 1997, 97, 2879-2932.
9. 1a
10. 2 complex of CP450; phen, 1,10-phenanthroline; RC, retention of configuration;
11. 3a,35c
12. (a) Ortiz de Montellano, P. R., Ed. Cytochrome P-450: Structure, Mechanism, and Biochemistry, 2nd ed.; Plenum: New York, 1995.
13. (b) Sono, M.; Roach, M. P.; Coulter, E. D.; Dowson, J. D. Heme-Containing Oxygenases. Chem. Rev. 1996, 96, 2841-2887.
14. (a) Wallar, B. J.; Lipscomb, J. D. Dioxygen Activation by Enzymes Containing Dinuclear Non-Heme Iron Clusters. Chem. Rev. 1996, 96, 2625-2657.
15. (b) Elango, N.; Radhakrishnan, R.; Froland, W. A.; Wallar, B. J.; Earhart, C. A.; Lipscomb, J. D.; Ohlendorf, D. H. Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b. Protein Sci. 1997, 6, 556-568.
16. IV Cluster. J. Am. Chem. Soc. 1993, 115, 6450-6451.
17. (a) Valentine, A. M.; Lippard, S. J. Principles of small molecule activation by metalloenzymes as exemplified by the soluble methane monooxygenase from Methylococcus capsulatus (Bath). J. Chem. Soc., Dalton Trans. 1997, 3925-3932.
18. (b) Rosenzweig, A. C.; Nordlund, P.; Takahara, P. M.; Frederick, C. A.; Lippard, S. J. Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states. Chem. Biol. 1995, 2, 409-418.
19. (c) Valentine, A. M.; Wilkinson, B.; Liu, K. E.; Komar-Panicucci, S.; Priestley, N. D.; Williams, P. G.; Morimoto, H.; Floss, H. G.; Lippard, S. J. Tritirated Chiral Alkanes as Substrates for sMMO from Methylococcus capsulatus (Bath): Probes for the Mechanism of Hydroxylation. J. Am. Chem. Soc. 1997, 119, 1818-1827.
20. (d) Lee, D.; Lippard, S. J. Structural and Functional Models of Dioxygen-Activating Centers of Non-Heme Enzymes RNR and sMMO. J. Am. Chem. Soc. 1998, 120, 12153-12154.
21. Jiang, Y.; Wilkins, P. C.; Dalton, H. Activation of the hydrxylase of sMMO from Methylococcus capsulatus (Bath) by hydrogen peroxide. Biochim. Biophys. Acta 1993, 1163, 105-112.
22. (a) Groves, J. T.; Han, Y. Z. Models and Mechanism of Cytochrome P-450 Action. In ref 7a, pp 3-48.
23. (b) Groves, J. T.; Viski, P. Asymmetric Hydroxylation by a Chiral Iron Porphyrin. J. Am. Chem. Soc. 1969, 111, 8537-8538.
24. (a) Que, L., Jr. Oxygen activation at non-heme diiron active sites in biology: lessons from model complexes. J. Chem. Soc., Dalton Trans. 1997, 3933-3940.
25. 2 Diamond Core Structure for the Key Intermediate Q of Methane Monooxygenase. Science 1997, 275, 515-518.
26. 2 Catalyzed by an Iron(II) Tris(2-pyridylmethyl)amine Complex. J. Am. Chem. Soc. 1997, 119, 5964-5965.
27. Newcomb, M.; Le-Tadic-Biadatti, M. H.; Chestney, D. L.; Roberts, E. S.; Hollenberg, P. F. A Nonsynchronous Concerted Mechanism for Cytochrome P-450 Catalyzed Hydroxylation. J. Am. Chem. Soc. 1995, 117, 12085-12091.
28. (a) Yoshizawa, K.; Yamabe, T.; Hoffmann, R. Possible intermediates for the conversion of methane to methanol on dinuclear iron centers of MMO models. New J. Chem. 1997, 21, 151-161.
29. (b) Siegbahn, P. E. M.; Crabtree, R. H. Mechanism of C-H Activation by MMO: Quantum Chemical Studies. J. Am. Chem. Soc. 1997, 119, 3103-3113.
30. Khenkin, A. M.; Shilov, A. E. Biomimetic alkane oxidation in the presence of iron complexes. New J. Chem. 1989, 13, 659-667.
31. (a) Sorokin, A. B.; Khenkin, A. M. Isotope Effect in Aliphatic Hydroxylation by a Cytochrome P-450 Models. J. Chem. Soc., Chem. Commun. 1990, 45-46.
32. (b) Sorokin, A.; Robert, A.; Meunier B. Intramolecular Kinetic Isotope Effects in Alkane Hydroxylations Catalyzed by Manganese and Iron Porphyrin Complexes. J. Am. Chem. Soc. 1993, 115, 7293-7299.
33. Karasevich, E. I.; Khenkin, A. M.; Shilov, A. E. A Chemical Model of Cytochrome P-450: Monooxygenase-like Activation of Dioxygen. J. Chem. Soc., Chem. Commun. 1987, 731-733.
34. Karasevich E. I.; Anisimova, B. L.; Rubailo, V. L.; Shilov, A. E. Kinetics of cyclohexane oxidation by molecular oxygen in the presence of iron porphyrins and reductant. Kinet. Katal. 1993, 34, 650-661.
35. Muradov, N. Z.; Shilov, A. E.; Shteinman, A. A. New models of monooxygenase on the basis of Sn(II) compounds. React. Kinet. Catal. Lett. 1975, 2, 417-423.
36. Kurtz, D. M., Jr. Oxo-and Hydroxo-Bridged Diiron Complexes: A Chemical Perspective on a Biological Unit. Chem. Rev. 1990, 90, 585-606.
37. (a) Shteinman, A. A. Synthesis and Properties of Dinuclear μ-Oxo-μ-Carboxylato Iron(III) Complexes with Labile Coordination Site. Mendeleev Commun. 1992, 155-157.
38. (b) Shteinman, A. A. Alkane oxidation catalyzed by μ-oxo-μ-carboxylato-diiron(III) dipyridine complexes. Dokl. Akad. Nauk SSSR 1991, 321, 775-779 [Dokl. Chem., 1991, No. 4 (Engl. Transl.)]
39. (b) Shteinman, A. A. Alkane oxidation catalyzed by μ-oxo-μ-carboxylato-diiron(III) dipyridine complexes. Dokl. Akad. Nauk SSSR 1991, 321, 775-779 [Dokl. Chem., 1991, No. 4 (Engl. Transl.)]
40. Gritsenko, O. N.; Nesterenko, G. N.; Shteinman A. A. Effect of substituents in the ligand on oxidation of alkanes catalyzed by dinuclear oxo-bridged iron complexes. Russ. Chem. Bull. 1995, 2415-2417.
41. Kulikova, V. S.; Gritsenko, O. N.; Shteinman, A. A. Molecular mechanism of alkane oxidation involving dinuclear iron complexes. Mendeleev Commun. 1996, 119-120.
42. No such effect was ever observed for chain radical oxidation.
43. Gritsenko, O. N.; Nesterenko, G. N.; Kulikova, V. S.; Shteinman, A. A. Hydrocarbon Oxidation by Hydroperoxides Catalyzed by Binuclear Fe(III) Complexes. Kinet. Catal. 1997, 38, 699-706.
44. Trukhan, V. M.; Polukhov, V. V.; Sulimenkov, I. V.; Ovanesyan, N. S.; Dodonov, A. F.; Shteinman, A. A. The first structural and functional model of MMO. Kinet. Catal. 1998, 39, 788-791.
45. Panov, G. I.; Uriarte, A. K.; Rodkin, M. A.; Sobolev, V. I. Generation of active oxygen species on solid surfaces. Catal. Today 1998, 41, 365-385.
46. Panov, G. I.; Sobolev, V. I.; Dubkov, K. A.; Parmon, V. N.; Ovanesyan, N. S.; Shilov, A. E.; Shteinman, A. A. Iron complexes in zeolites as a new model of methane monooxygenase. React. Kinet. Catal. Lett. 1997, 61, 251-258.
47. Dubkov, K. A.; Sobolev, V. I.; Talsi, E. P.; Rodkin, M. A.; Watkins, N. H.; Shteinman, A. A.; Panov, G. I. Kinetic isotope effects and mechanism of biomimetic oxidation of methane and benzene on FeZSM-5 zeolite. J. Mol. Catal.: A 1997, 123, 155-161.
48. Ovanesyan, N. S.; Sobolev, V. I.; Dubkov, K. A.; Panov, G. I.; Shteinman, A. A. The nature of the active oxidant in biomimetic oxidation of methane over FeZSM-5 zeolite. Russ. Chem. Bull. 1996, 45, 1509-1510.
49. 2O system. Kinet. Catal. 1998, 39, 792-796.
50. cam with m-Chloroperbenzoic Acid. Biochem. Biophys. Res. Commun. 1994, 201, 1464-1469.
51. Weiss, R. Oxoiron Porphyrin Species with High-Valent Iron. Angew. Chem., Int. Ed. Engl. 1989, 28, 1709-1712.
52. 2 activation by Cytochrome P-450. Chem. Commun. 1984, 1219-1220; Oxid. Commun. 1983, 4, 433-441.
53. 2 activation by Cytochrome P-450. Chem. Commun. 1984, 1219-1220; Oxid. Commun. 1983, 4, 433-441.
54. (a) Shteinman, A. A. The mechanism of methane and dioxygen activation in the catalytic cycle of methane monooxygenase. FEBS Lett. 1995 362, 5-9; Russ. Chem. Bull. 1995, 44, 975-984.
55. (a) Shteinman, A. A. The mechanism of methane and dioxygen activation in the catalytic cycle of methane monooxygenase. FEBS Lett. 1995 362, 5-9; Russ. Chem. Bull. 1995, 44, 975-984.
56. 2 activation at the active center of methane monooxygenase. Russ. Chem. Bull. 1997, 46, 1599-1605.
57. (c) Shteinman, A. A. Does the non-heme monooxygenase sMMO share a unified oxidation mechanism with the heme monooxygenase cytochrome P-450? J. Biol. Inorg. Chem. 1998, 3, 325-330.
58. (a) Shestakov, A. F.; Shilov, A. E. Five-coordinate carbon hydroxylation mechanism. J. Mol. Catal. A 1996, 105, 1-7; Russ. J. Gen. Chem. 1995, 65, 559-569.
59. (a) Shestakov, A. F.; Shilov, A. E. Five-coordinate carbon hydroxylation mechanism. J. Mol. Catal. A 1996, 105, 1-7; Russ. J. Gen. Chem. 1995, 65, 559-569.
60. (b) Karasevich, E. I.; Shestakov, A. F.; Shilov, A. E. Catalytic alkane hydroxylation via five-coordinate carbon intermediate: dynamic aspects. Kinet. Katal. 1997, 38, 782-789.
61. Lin, M.; Hogan, T. E.; Sen, A. Catalytic Carbon-Carbon and Carbon-Hydrogen Bond Cleavage in Lower Alkanes. Low-Temperature Hydroxylations and Hydroxycarbonylations with Dioxygen as the Oxidant. J. Am. Chem. Soc. 1996, 118, 4574-4580.