Literature DB >> 16871510

Substitution of hydrogen by deuterium changes the regioselectivity of ethylbenzene hydroxylation by an oxo-iron-porphyrin catalyst.

Sam P de Visser1.   

Abstract

Heme oxo-iron complexes are powerful oxygenation catalysts of environmentally benign hydroxylation processes. We have performed density functional theoretic calculations on a model system, that is, an oxo-iron-porphyrin (Por) complex [(Fe=O)Cl(Por)], and studied its reactivity toward a realistic substrate, namely, ethylbenzene. The calculations showed that the dominant reaction process in the gas phase is benzyl hydroxylation leading to 1-phenylethanol, with an energetic barrier of 9.1 kcal mol(-1), while the competing para-phenyl hydroxylation has a barrier 3.0 kcal mol(-1) higher in energy. This benzyl hydroxylation barrier is the lowest C-H hydroxylation barrier we have obtained so far for oxo-iron-porphyrin complexes. Due to electronic differences between the intermediates in the phenyl and benzyl hydroxylation processes, the phenyl hydroxylation process is considerably stabilised over the benzyl hydroxylation mechanism in environments with a large dielectric constant. In addition, we calculated kinetic isotope effects of the substitution of one or more hydrogen atoms of ethylbenzene by deuterium atoms and studied its effect on the reaction barriers. Thus, in a medium with a large dielectric constant, a regioselectivity change occurs between [H(10)]ethylbenzene and [D(10)]ethylbenzene whereby the deuterated species gives phenol products whereas the hydrogenated species gives mainly 1-phenylethanol products. This remarkable metabolic switching was analysed and found to occur due to 1) differences in strength between a C-H versus a C-D bond and 2) stabilisation of cationic intermediates in a medium with a large dielectric constant. We have compared our calculations with experimental work on synthetic oxo-iron-porphyrin catalysts as well as with enzyme-reactivity studies.

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Year:  2006        PMID: 16871510     DOI: 10.1002/chem.200600376

Source DB:  PubMed          Journal:  Chemistry        ISSN: 0947-6539            Impact factor:   5.236


  14 in total

1.  Axial and equatorial ligand effects on biomimetic cysteine dioxygenase model complexes.

Authors:  Luis E Gonzalez-Ovalle; Matthew G Quesne; Devesh Kumar; David P Goldberg; Sam P de Visser
Journal:  Org Biomol Chem       Date:  2012-06-19       Impact factor: 3.876

2.  Mechanism of S-oxygenation by a cysteine dioxygenase model complex.

Authors:  Devesh Kumar; G Narahari Sastry; David P Goldberg; Sam P de Visser
Journal:  J Phys Chem A       Date:  2011-12-12       Impact factor: 2.781

3.  Arene activation by a nonheme iron(III)-hydroperoxo complex: pathways leading to phenol and ketone products.

Authors:  Abayomi S Faponle; Frédéric Banse; Sam P de Visser
Journal:  J Biol Inorg Chem       Date:  2016-04-20       Impact factor: 3.358

4.  Singlet versus Triplet Reactivity in an Mn(V)-Oxo Species: Testing Theoretical Predictions Against Experimental Evidence.

Authors:  Tzuhsiung Yang; Matthew G Quesne; Heather M Neu; Fabián G Cantú Reinhard; David P Goldberg; Sam P de Visser
Journal:  J Am Chem Soc       Date:  2016-09-14       Impact factor: 15.419

5.  Regioselectivity of substrate hydroxylation versus halogenation by a nonheme iron(IV)-oxo complex: possibility of rearrangement pathways.

Authors:  Matthew G Quesne; Sam P de Visser
Journal:  J Biol Inorg Chem       Date:  2012-05-13       Impact factor: 3.358

6.  Alkyl Chain Growth on a Transition Metal Center: How Does Iron Compare to Ruthenium and Osmium?

Authors:  Mala A Sainna; Sam P de Visser
Journal:  Int J Mol Sci       Date:  2015-09-28       Impact factor: 5.923

7.  Differences and comparisons of the properties and reactivities of iron(III)-hydroperoxo complexes with saturated coordination sphere.

Authors:  Abayomi S Faponle; Matthew G Quesne; Chivukula V Sastri; Frédéric Banse; Sam P de Visser
Journal:  Chemistry       Date:  2014-11-14       Impact factor: 5.236

8.  How Are Substrate Binding and Catalysis Affected by Mutating Glu127 and Arg161 in Prolyl-4-hydroxylase? A QM/MM and MD Study.

Authors:  Amy Timmins; Sam P de Visser
Journal:  Front Chem       Date:  2017-11-09       Impact factor: 5.221

9.  Nitrogen Reduction to Ammonia on a Biomimetic Mononuclear Iron Centre: Insights into the Nitrogenase Enzyme.

Authors:  Monika A Kaczmarek; Abheek Malhotra; G Alex Balan; Amy Timmins; Sam P de Visser
Journal:  Chemistry       Date:  2017-12-14       Impact factor: 5.236

Review 10.  Challenging Density Functional Theory Calculations with Hemes and Porphyrins.

Authors:  Sam P de Visser; Martin J Stillman
Journal:  Int J Mol Sci       Date:  2016-04-07       Impact factor: 5.923

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