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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F16%3A00458875" target="_blank" >RIV/61388955:_____/16:00458875 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1021/jacs.6b01151" target="_blank" >http://dx.doi.org/10.1021/jacs.6b01151</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/jacs.6b01151" target="_blank" >10.1021/jacs.6b01151</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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 FeIV═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 FeIV═O intermediate with Br– ligation contain information-rich features that largely parallel the corresponding spectra of the S = 2 model complex (TMG3tren)FeIV═O (Srnec, M.; Wong, S. D.; England, J.; Que, L. Jr.; 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 FeIV═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–FeIV═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 FeIV═O at the transition states resulting from the weaker ligand field of the halogenase.

Název v anglickém jazyce

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

Popis výsledku anglicky

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 FeIV═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 FeIV═O intermediate with Br– ligation contain information-rich features that largely parallel the corresponding spectra of the S = 2 model complex (TMG3tren)FeIV═O (Srnec, M.; Wong, S. D.; England, J.; Que, L. Jr.; 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 FeIV═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–FeIV═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 FeIV═O at the transition states resulting from the weaker ligand field of the halogenase.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

—

Projekt

<a href="/cs/project/GJ15-10279Y" target="_blank" >GJ15-10279Y: Redoxní vlastnosti a reaktivita nehemových aktivních center se železem</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2016

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of the American Chemical Society

ISSN

0002-7863

e-ISSN

—

Svazek periodika

138

Číslo periodika v rámci svazku

15

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

13

Strana od-do

5110-5122

Kód UT WoS článku

000374812100020

EID výsledku v databázi Scopus

2-s2.0-84966417260