Frontier Molecular Orbital Contributions to Chlorination versus Hydroxylation Selectivity in the Non-Heme Iron Halogenase SyrB2

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F17%3A00471846" target="_blank" >RIV/61388955:_____/17:00471846 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1021/jacs.6b11995" target="_blank" >http://dx.doi.org/10.1021/jacs.6b11995</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/jacs.6b11995" target="_blank" >10.1021/jacs.6b11995</a>

Result language

angličtina

Original language name

Frontier Molecular Orbital Contributions to Chlorination versus Hydroxylation Selectivity in the Non-Heme Iron Halogenase SyrB2

Original language description

The ability of an Fe-IV=O intermediate in SyrB2 to perform chlorination versus hydroxylation was computationally evaluated for different substrates that had been Studied experimentally. The pi-trajectory for H atom abstraction (Fe-IV=O oriented perpendicular to the C-H bond of substrate) was found to lead to the S = 2 five-coordinate HO-Fe-III-Cl complex with the C-center dot of the substrate, pi-oriented relative to both the Cl- and the OH- ligands. From this ferric intermediate, hydroxylation is thermodynamically faVored, but chlorination is intrinsically more reactive due to the energy splitting between two key redox-active d pi* frontier Molecular orbitals (FMOs). The splitting is determined by the differential ligand field effect of Cl- OH- versus on the Fe center. This makes chlorination effectively competitive with hydroxylation. Chlorination versus hydroxylation selectivity is then determined by the orientation of the substrate with respect to the HO-Fe-Cl plane that controls either the Cl- or the OH- to rebound depending on the relative pi-overlap with the substrate C radical. The differential contribution of the two FMOs to chlorination versus hydroxylation selectivity in SyrB2 is related to reaction mechanism that involves two asynchronous transfers: electron transfer from the substrate radical to the iron center followed by late ligand (Cl- or OH-) transfer to the substrate.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10403 - Physical chemistry

Project

<a href="/en/project/GJ15-10279Y" target="_blank" >GJ15-10279Y: Redox properties and reactivities of nonheme iron active sites</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2017

Confidentiality

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

Name of the periodical

Journal of the American Chemical Society

ISSN

0002-7863

e-ISSN

—

Volume of the periodical

139

Issue of the periodical within the volume

6

Country of publishing house

US - UNITED STATES

Number of pages

12

Pages from-to

2396-2407

UT code for WoS article

000394482200042

EID of the result in the Scopus database

2-s2.0-85013059462