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Low temperature magnetic circular dichroism (LT MCD) spectroscopy in combination with quantum-chemical calculations are used to define the electronic structure associated with the geometric structure of the Fe(IV)═O intermediate in SyrB2 that was previously determined by nuclear resonance vibrational spectroscopy. These studies elucidate key frontier molecular orbitals (FMOs) and their contribution to H atom abstraction reactivity. The VT MCD spectra of the enzymatic S = 2 Fe(IV)═O intermediate with Br(-) ligation contain information-rich features that largely parallel the corresponding spectra of the S = 2 model complex (TMG3tren)Fe(IV)═O (Srnec, M.; Wong, S. D.; England, J; Que, L; Solomon, E. I. Proc. Natl. Acad. Sci. USA 2012, 109, 14326-14331). However, quantitative differences are observed that correlate with π-anisotropy and oxo donor strength that perturb FMOs and affect reactivity. Due to π-anisotropy, the Fe(IV)═O active site exhibits enhanced reactivity in the direction of the substrate cavity that proceeds through a π-channel that is controlled by perpendicular orientation of the substrate C-H bond relative to the halide-Fe(IV)═O plane. Also, the increased intrinsic reactivity of the SyrB2 intermediate relative to the ferryl model complex is correlated to a higher oxyl character of the Fe(IV)═O at the transition states resulting from the weaker ligand field of the halogenase.

Competing Interests: Notes The authors declare no competing financial interest

Titel:	Electronic Structure of the Ferryl Intermediate in the α-Ketoglutarate Dependent Non-Heme Iron Halogenase SyrB2: Contributions to H Atom Abstraction Reactivity.
Autor/in / Beteiligte Person:	Srnec, M ; Wong, SD ; Matthews, ML ; Krebs, C ; Bollinger JM Jr ; Solomon, EI
Link:	Zum Volltext
Zeitschrift:	Journal of the American Chemical Society, Jg. 138 (2016-04-20), Heft 15, S. 5110-22
Veröffentlichung:	Washington, DC : American Chemical Society ; <i>Original Publication</i>: Easton, Pa. [etc.], 2016
Medientyp:	academicJournal
ISSN:	1520-5126 (electronic)
DOI:	10.1021/jacs.6b01151
Schlagwort:	Bacterial Proteins chemistry Bacterial Proteins metabolism Circular Dichroism Glutarates metabolism Iron Compounds metabolism Models, Molecular Nonheme Iron Proteins metabolism Oxidoreductases metabolism Quantum Theory Threonine chemistry Threonine metabolism Glutarates chemistry Hydrogen chemistry Iron Compounds chemistry Nonheme Iron Proteins chemistry Oxidoreductases chemistry
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. Language: English [J Am Chem Soc] 2016 Apr 20; Vol. 138 (15), pp. 5110-22. <i>Date of Electronic Publication: </i>2016 Apr 12. MeSH Terms: Glutarates / chemistry ; Hydrogen / chemistry ; Iron Compounds / chemistry ; Nonheme Iron Proteins / chemistry ; Oxidoreductases / *chemistry ; Bacterial Proteins / chemistry ; Bacterial Proteins / metabolism ; Circular Dichroism ; Glutarates / metabolism ; Iron Compounds / metabolism ; Models, Molecular ; Nonheme Iron Proteins / metabolism ; Oxidoreductases / metabolism ; Quantum Theory ; Threonine / chemistry ; Threonine / metabolism References: Nat Chem. 2011 Jan;3(1):19-27. (PMID: 21160512) ; Proc Natl Acad Sci U S A. 2009 Oct 20;106(42):17723-8. (PMID: 19815524) ; Biochemistry. 2009 May 26;48(20):4331-43. (PMID: 19245217) ; Proc Natl Acad Sci U S A. 2012 Sep 4;109(36):14326-31. (PMID: 22908238) ; Phys Rev A Gen Phys. 1989 Jun 1;39(11):6016-6017. (PMID: 9901188) ; Biochemistry. 2011 Mar 22;50(11):1928-33. (PMID: 21261288) ; Inorg Chem. 1999 Apr 19;38(8):1847-1865. (PMID: 11670957) ; J Am Chem Soc. 2010 Jun 30;132(25):8635-44. (PMID: 20568768) ; Proc Natl Acad Sci U S A. 2006 Aug 29;103(35):12966-73. (PMID: 16920789) ; J Am Chem Soc. 2007 Nov 7;129(44):13408-9. (PMID: 17939667) ; PLoS Comput Biol. 2012;8(10):e1002708. (PMID: 23093919) ; Chem Commun (Camb). 2014 Sep 25;50(74):10887-90. (PMID: 25093575) ; J Comput Chem. 2006 Nov 30;27(15):1787-99. (PMID: 16955487) ; Proc Natl Acad Sci U S A. 2011 Jan 25;108(4):1228-33. (PMID: 21220293) ; Phys Rev A Gen Phys. 1986 Jun;33(6):3742-3748. (PMID: 9897114) ; J Comput Chem. 2004 Sep;25(12):1463-73. (PMID: 15224390) ; J Inorg Biochem. 2006 Apr;100(4):697-706. (PMID: 16510189) ; Acc Chem Res. 2013 Nov 19;46(11):2725-39. (PMID: 24070107) ; J Am Chem Soc. 2007 Sep 19;129(37):11334-5. (PMID: 17715926) ; Proc Natl Acad Sci U S A. 2005 Jul 19;102(29):10111-6. (PMID: 16002467) ; J Am Chem Soc. 2011 Aug 10;133(31):11880-3. (PMID: 21739994) ; J Am Chem Soc. 2004 Jul 7;126(26):8108-9. (PMID: 15225039) ; J Comput Chem. 2010 Jan 15;31(1):224-47. (PMID: 19499541) ; Nature. 2006 Mar 16;440(7082):368-71. (PMID: 16541079) ; Inorg Chem. 2005 Dec 12;44(25):9592-6. (PMID: 16323949) ; Nature. 2013 Jul 18;499(7458):320-3. (PMID: 23868262) ; Biochemistry. 2003 Jun 24;42(24):7497-508. (PMID: 12809506) ; Nat Chem Biol. 2007 Feb;3(2):113-6. (PMID: 17220900) ; J Am Chem Soc. 2004 May 5;126(17):5378-9. (PMID: 15113207) ; J Am Chem Soc. 2010 Sep 8;132(35):12188-90. (PMID: 20704272) ; J Am Chem Soc. 2004 Jan 21;126(2):472-3. (PMID: 14719937) ; Chem Sci. 2014 Mar 1;5(3):1204-1215. (PMID: 24660055) ; J Am Chem Soc. 2008 Sep 17;130(37):12394-407. (PMID: 18712873) ; Proc Natl Acad Sci U S A. 2006 Oct 3;103(40):14738-43. (PMID: 17003127) ; J Am Chem Soc. 2011 Nov 16;133(45):18148-60. (PMID: 21981763) ; Angew Chem Int Ed Engl. 2010 Mar 29;49(14 ):2622-5. (PMID: 20229541) ; J Am Chem Soc. 2015 Feb 25;137(7):2428-31. (PMID: 25674662) ; Science. 2014 Mar 7;343(6175):1140-4. (PMID: 24604200) ; Phys Rev A Gen Phys. 1988 Sep 15;38(6):3098-3100. (PMID: 9900728) ; Inorg Chem. 2006 Aug 7;45(16):6435-45. (PMID: 16878956) ; Chem Rev. 2011 Nov 9;111(11):6513-56. (PMID: 21861478) ; J Am Chem Soc. 2007 Dec 26;129(51):15983-96. (PMID: 18052249) Grant Information: R01 GM040392 United States GM NIGMS NIH HHS; R01 GM069657 United States GM NIGMS NIH HHS; R01GM040392 United States GM NIGMS NIH HHS; R01GM69657 United States GM NIGMS NIH HHS Substance Nomenclature: 0 (Bacterial Proteins) ; 0 (Glutarates) ; 0 (Iron Compounds) ; 0 (Nonheme Iron Proteins) ; 11140-67-3 (syringomycin) ; 2ZD004190S (Threonine) ; 7YNJ3PO35Z (Hydrogen) ; EC 1.- (Oxidoreductases) Entry Date(s): Date Created: 20160330 Date Completed: 20161109 Latest Revision: 20181113 Update Code: 20231215 PubMed Central ID: PMC4927264

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Electronic Structure of the Ferryl Intermediate in the α-Ketoglutarate Dependent Non-Heme Iron Halogenase SyrB2: Contributions to H Atom Abstraction Reactivity.