New insight into reaction of iron(III)-peroxide adduct with alkanes: An alternative model for cytochrome P-450 and methane monooxygenase

Zeitschrift fur Naturforschung Section C - Journal of Biosciences

Volumn 52, Issue 9-10, 1997, Pages 615-622

  Nishida, Yuzo ^a   Ito, Sayo ^a   Okuno, Takashi ^a   Ohba, Shigeru ^a  

^a NONE

Author keywords

Activation of Peroxide Adduct; Alkane Functionalization; Electrophilicity of Metal peroxide; Iron(III) peroxide Adduct

Indexed keywords

EID: 0030779583     PISSN: 09395075     EISSN: None     Source Type: Journal    
DOI: 10.1515/znc-1997-9-1008     Document Type: Article

References (36)

1. Bach R. D., Mintcheva I., Esteva C. M. and Schlegel H. B. (1995), Theoretical model for an alternative mechanism for the cytochrome P-450 hydroxylation of quadricyclane. J. Am. Chem. Soc. 117, 10121-10122.
2. Bach R. D. and Su M.-D. (1994), The transition state for the hydroxylation of saturated hydrocarbons with hydroperoxonium ion. J. Am. Chem. Soc. 116, 10103-10109.
3. Feig A. L. and Lippard S. J. (1994), Reactions of nonheme iron(II) centers with dioxygen in biology and chemistry. Chem. Rev. 94, 759-805.
4. Groves A. J. and Nemo T. E. (1983), Epoxidation reactions catalyzed by iron porphyrins. Oxygen transfer from iodosylbenzene. J. Am. Chem. Soc. 105, 5786-5791.
5. Gunter M. J. and Turner P. (1991), Metalloporphyrins as models for cytochromes P-450. Coord. Chem. Rev. 108, 115-161.
6. Hill C. L. (1989), Activation and Functionalization of Alkanes. John-Wiley & Sons, New York.
7. cam oxygen activation. J. Am. Chem. Soc. 116, 11671-11674.
8. Hoffmann R., Chen M. M.-L. and Thorn D. L. (1977), Qualitative discussion of alternative coordination modes of diatomic ligands in transition metal complexes. Inorg. Chem. 16, 503-511.
9. cam monooxygenase activity by a single mutation, threonine-252 to alanine or valine: possible role of the hydroxy amino acid in oxygen activation. Proc. Natl. Acad. Sci. U.S.A. 86, 7823-7827.
10. 2 catalyzed by dinuclear iron(III) complexes with amide-containing ligands. J. Chem. Soc., Dalton Trans. 4479-4484.
11. Ito S., Suzuki M., Kobayashi T., Ohba S. and Nishida Y. (1996b), Formation and reactivity of a peroxide adduct of iron(III) complexes containing substituted phenol derivatives. J. Chem. Soc., Dalton Trans. 2579-2580.
12. Kimata Y., Shimada H., Hirose T. and Ishimura Y. (1995), Role of Thr-252 in cytochrome P-450CAM; a study with unnatural amino acid mutagenesis. Biochem. Biophys. Res. Commun. 208, 96-102.
13. Kojima T., Leising R. A., Yan S. and Que L. jr. (1993), Alkane functionalization at nonheme iron centers; stoichiometric transfer of metal-bound ligand to alkane. J. Am. Chem. Soc. 115, 11328-11335.
14. Leising R. A., Kim J., Perez M. A. and Que L., Jr. (1993), Alkane functionalization at (μ-oxy)diiron(III) centers. J. Am. Chem. Soc. 115, 9524-9530.
15. Lipscomb J. D. (1994), Biochemistry of the soluble methane monooxygenase. Annu. Rev. Microbiol. 48, 371-399.
16. Liu K. E., Valentine A. M., Wang D., Huynh B. H., Edmondson D. E., Salifoglou A. and Lippard S. J. (1995), Kinetic and spectroscopic characterization of intermediates and component interaction in reactions of methane monooxygenase from Methylcoccus capsulatus. J. Am. Chem. Soc. 117, 10174-10185.
17. 2; monooxygenase- and catalase-like activities. J. Chem. Soc., Dalton Trans. 2081-2084.
18. Montellano P. R. (1986), Cytochrome P-450. Plenum Press, New York.
19. Newcomb M., Tadic M.-H., Putt D. M. and Hollenberg P. E. (1995), A nonsynchronous concerted mechanism for cytochrome P-450 catalyzed hydroxylation. J. Am. Chem. Soc. 117, 12985-12091.
20. Nishida Y., Itoh H. and Yamazaki A. (1994), On the chemical mechanism of aldehyde metabolism by cytochrome P-450. Polyhedron 13, 2473-2476.
21. Nishida Y., Okuno T., Ito S., Ohba S., Matsushima H. and Tokii T. (1995), Important role of tetrahydrofuran ring in activation of hydrogen peroxide in the presence of binuclear iron(III) complexes with linear μ-oxo bridge. Chem. Lett. 885-886.
22. Nishida Y. and Ito S. (1995a), High activity of an Fe-tfda complex for hydroxylation at the aromatic and alkane rings of 2′-deoxyguanosine in the presence of hydrogen peroxide. J. Chem. Soc., Chem. Commun. 1211-1212.
23. Nishida Y. and Ito S. (1995b), Comparison on reactivity of Fe(III) and Al(I) compounds in the presence of hydrogen peroxide; its relevance to possible origin for central nervous system by aluminium ion. Z. Naturforsch. 50c, 571-577.
24. Peng, H-Ming, Raner G. M., Vaz A. D. N. and Coon M. J. (1995), Oxidative cleavage of esters and amides to carbonyl compounds by cytochrome P-450. Arch. Biochem. Biophys. 318, 333-339.
25. CAM. J. Mol. Biol. 195, 687-700.
26. 3+ complex. J. Chem. Soc., Chem. Commun. 2297-2298.
27. CAM active site mutant Thr252Ala. Biochemistry 30, 11420-11429.
28. Rana T. M. and Meares C. F. (1991), Transfer of oxygen from an artificial protease to peptide carbon during proteolysis. Proc. Natl. Acad. Sci. USA 88, 10578-10582.
29. Schroder D., Schalley C. A., Goldberg N., Hrusak J. and Schwarz H. (1996), Gas-phase experiments aimed at probing the existence of the elusive water oxide molecule. Chem. Eur. J. 2, 1235-1242.
30. 2 diamond core structure for the key intermediate Q of methane monooxygenase. Science 275, 515-518.
31. Sono M., Roach M. P., Coulter E. D. and Dawson J. H. (1996), Heme-containing oxygenases. Chem. Rev. 96, 2841-2887.
32. Sturgeon B. E., Burdi D., Chen S., Huynh B.-H., Edmondson D. E., Stubbe J. and Hoffman B. M. (1996), Reconsideration of X, the diiron intermediate formed during cofactor assembly in E. coli ribonucleotide reductase. J. Am. Chem. Soc. 118, 7551-7557.
33. 2. J. Chem. Soc., Dalton Trans. 2375-2380.
34. Torpey J., Lee D. A., Smith K. M. and Monteifano P. R. (1996), Oxidation of an α-meso-methyl-substituted heme to an α-biliverdin by heme-oxygenase. A novel heme cleavage reaction. J. Am. Chem. Soc. 118, 9172-9173.
35. Vaz A. D. N., Pernecky S. J., Raner G. M. and Coon M. J. (1996), Peroxo-iron and oxenoid species as alternative oxygenating agents in cytochrome P-450-catalyzed reactions. Switching by threonine-302 to alanine mutagenesis of cytochrome P-450 2B4. Proc. Natl. Acad. Sci. U.S.A. 93, 4644-4648.
36. Waller B. J. and Lipscomb J. D. (1996), Dioxygen activation by enzymes containing binuclear non-heme iron clusters. Chem. Rev. 96, 2625-2657.