Electronic Structure of the Ferryl Intermediate in the α-Ketoglutarate Dependent Non-Heme Iron Halogenase SyrB2: Contributions to H Atom Abstraction Reactivity
The result's identifiers
Result code in 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>
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Electronic Structure of the Ferryl Intermediate in the α-Ketoglutarate Dependent Non-Heme Iron Halogenase SyrB2: Contributions to H Atom Abstraction Reactivity
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GJ15-10279Y" target="_blank" >GJ15-10279Y: Redox properties and reactivities of nonheme iron active sites</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of the American Chemical Society
ISSN
0002-7863
e-ISSN
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Volume of the periodical
138
Issue of the periodical within the volume
15
Country of publishing house
US - UNITED STATES
Number of pages
13
Pages from-to
5110-5122
UT code for WoS article
000374812100020
EID of the result in the Scopus database
2-s2.0-84966417260