Two interconverting Fe(IV) intermediates in aliphatic chlorination by the halogenase CytC3

Nature Chemical Biology

Volumn 3, Issue 2, 2007, Pages 113-116

  Galonić, Danica P ^a   Barr, Eric W ^b   Walsh, Christopher T ^a   Bollinger, J Martin ^b   Krebs, Carsten ^b  

^a HARVARD MEDICAL SCHOOL   (United States)

^b PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINOBUTYRIC ACID DERIVATIVE; ENZYME; IRON; METHYL GROUP; OXYGENASE; PROTEIN; PROTEIN CYTC2; PROTEIN CYTC3; UNCLASSIFIED DRUG;

ARTICLE; CHLORINATION; PRIORITY JOURNAL; SOIL; STREPTOMYCES;

STREPTOMYCES SP.;

AMINOBUTYRIC ACIDS; CARRIER PROTEINS; CATALYTIC DOMAIN; CHLORINE; DEUTERIUM; IRON; KETOGLUTARIC ACIDS; KINETICS; MODELS, CHEMICAL; NONHEME IRON PROTEINS; OXIDATION-REDUCTION; OXIDOREDUCTASES; OXYGEN; SPECTROPHOTOMETRY, ULTRAVIOLET; SPECTROSCOPY, MOSSBAUER; STREPTOMYCES;

EID: 33846379972     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio856     Document Type: Article

References (32)

1. Gribble, G.W. Naturally occurring organohalogen compounds. Acc. Chem. Res. 31, 141-152 (1998).
2. van Pee, K.-H. & Unversucht, S. Biological dehalogenation and halogenation reactions. Chemosphere 52, 299-312 (2003).
3. Butler, A. & Carter-Franklin, J.N. The role of vanadium bromoperoxidase in the biosynthesis of halogenated marine natural products. Nat. Prod. Rep. 21, 180-188 (2004).
4. Gribble, G.W. Natural organohalogens: a new frontier for medicinal agents? J. Chem. Educ. 81, 1441-1449 (2004).
5. Fenical, W. & Jensen, P.R. Developing a new resource for drug discovery: marine actinomycete bacteria. Nat. Chem. Biol. 2, 666-673 (2006).
6. 2-dependent halogenase. Proc. Natl. Acad. Sci. USA 102, 10111-10116 (2005).
7. Vaillancourt, F.H., Yeh, E., Vosburg, D.A., Garneau-Tsodikova, S. & Walsh, C.T. Nature's inventory of halogenation catalysts: oxidative strategies predominate. Chem. Rev. 106, 3364-3378 (2006).
8. Galonić, D.P., Vaillancourt, F.H. & Walsh, C.T. Halogenation of unactivated carbon centers in natural product biosynthesis: trichlorination of leucine during barbamide biosynthesis. J. Am. Chem. Soc. 128, 3900-3901 (2006).
9. Vaillancourt, F.H., Yeh, E., Vosburg, D.A., O'Connor, S.E. & Walsh, C.T. Cryptic chlorination by a non-haem iron enzyme during cyclopropyl amino acid biosynthesis. Nature 436, 1191-1194 (2005).
10. Ueki, M. et al. Enzymatic generation of the antimetabolite γ,γ-dichloroaminobutyrate by NRPS and mononuclear iron halogenase action in a Streptomycete. Chem. Biol. 13, 1183-1191 (2006).
11. Solomon, E.I. et al. Geometric and electronic structure/function correlations in nonheme iron enzymes. Chem. Rev. 100, 235-349 (2000).
12. Hausinger, R.P. Fe(II)/α-ketoglutarate-dependent hydroxylases and related enzymes. Crit. Rev. Biochem. Mol. Biol. 39, 21-68 (2004).
13. Costas, M., Mehn, M.P., Jensen, M.P. & Que, L., Jr. Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates. Chem. Rev. 104, 939-986 (2004).
14. Hanauske-Abel, H.M. & Günzler, V. A stereochemical concept for the catalytic mechanism of prolylhydroxylase. Applicability to classification and design of inhibitors. J. Theor. Biol. 94, 421-455 (1982).
15. Price, J.C., Barr, E.W., Tirupati, B., Bollinger, J.M., Jr. & Krebs, C. The first direct characterization of a high-valent iron intermediate in the reaction of an α-ketoglutarate-dependent dioxygenase: a high-spin Fe(IV) complex in taurine/α-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry 42, 7497-7508 (2003).
16. Price, J.C., Barr, E.W., Glass, T.E., Krebs, C. & Bollinger, J.M., Jr. Evidence for hydrogen abstraction from C1 of taurine by the high-spin Fe(IV) intermediate detected during oxygen activation by taurine:α-ketoglutarate dioxygenase (TauD). J. Am. Chem. Soc. 125, 13008-13009 (2003).
17. Bollinger, J.M., Jr. & Krebs, C. Stalking intermediates in oxygen activation by iron enzymes: motivation and method. J. Inorg. Biochem. 100, 586-605 (2006).
18. Proshlyakov, D.A., Henshaw, T.F., Monterosso, G.R., Ryle, M.J. & Hausinger, R.P. Direct detection of oxygen intermediates in the non-heme Fe enzyme taurine/α-ketoglutarate dioxygenase. J. Am. Chem. Soc. 126, 1022-1023 (2004).
19. Riggs-Gelasco, P.J. et al. EXAFS spectroscopic evidence for an Fe=O unit in the Fe(IV) intermediate observed during oxygen activation by taurine:α-ketoglutarate dioxygenase. J. Am. Chem. Soc. 126, 8108-8109 (2004).
20. Price, J.C., Barr, E.W., Hoffart, L.M., Krebs, C. & Bollinger, J.M., Jr. Kinetic dissection of the catalytic mechanism of taurine:α- ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry 44, 8138-8147 (2005).
21. Hoffart, L.M., Barr, E.W., Guyer, R.B., Bollinger, J.M., Jr. & Krebs, C. Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a prolyl-4-hydroxylase. Proc. Natl. Acad. Sci. USA 103, 14738-14743 (2006).
22. Blasiak, L.C., Vaillancourt, F.H., Walsh, C.T. & Drennan, C.L. Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis. Nature 440, 368-371 (2006).
23. Koehntop, K.D., Emerson, J.P. & Que, L., Jr. The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes. J. Biol. Inorg. Chem. 10, 87-93 (2005).
24. Quadri, L.E.N. et al. Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases. Biochemistry 37, 1585-1595 (1998).
25. Pavel, E.G. et al. Circular dichroism and magnetic circular dichroism spectroscopic studies of the non-heme ferrous active site in clavaminate synthase and its interaction with α-ketoglutarate cosubstrate. J. Am. Chem. Soc. 120, 743-753 (1998).
26. 57Fe Mössbauer spectroscopy: monitoring changes of an iron-containing active site during a biochemical reaction. Inorg. Chem. 44, 742-757 (2005).
27. IV=O: spectroscopic identification and oxo-group exchange. Angew. Chem. Int. Ed. 44, 6871-6874 (2005).
28. 2- and α-ketoglutarate- dependent tyrosyl radical formation in TauD, an α-keto acid-dependent non-heme iron dioxygenase. Biochemistry 42, 1854-1862 (2003).
29. Liu, P. et al. Oxygenase activity in the self-hydroxylation of (S)-2-hydroxypropylphosphonic acid epoxidase involved in fosfomycin biosynthesis. J. Am. Chem. Soc. 126, 10306-10312 (2004).
30. 2+ complexes in their lowest triplet and quintet states using multireference ab initio and density functional theory methods. J. Inorg. Biochem. 100, 716-726 (2006).
31. Kojima, T., Leising, R.A., Yan, S. & Que, L., Jr. Alkane functionalization at nonheme iron centers. Stoichiometric transfer of metal-bound ligands to alkane. J. Am. Chem. Soc. 115, 11328-11335 (1993).
32. Burzlaff, N.I. et al. The reaction cycle of isopenicillin N synthase observed by X-ray diffraction. Nature 401, 721-724 (1999).