Comparison of heme and nonheme iron-based 1-aminocyclopropane-1-carboxylic acid oxidase mimics: kinetic, mechanistic and computational studies
Author:
Affiliation:
1. Department of Chemistry
2. University of Pannonia
3. H-8200 Veszprém
4. Hungary
5. Babes-Bolyai University
6. RO-400024 Cluj-Napoca
7. Romania
8. Aix-Marseille Université
9. CNRS
10. Central Marseille
11. iSm2 UMR 7313
12. Marseille
Abstract
Kinetic, mechanistic and computational studies of the H2O2oxidation of 1-aminocyclopropane-1-carboxylic acid to ethylene by heme- and nonheme-type iron complexes are described as biomimics of 1-aminocyclopropane-1-carboxylic acid oxidase.
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemical Engineering,General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2015/RA/C4RA08762C
Reference47 articles.
1. Non-Heme Fe(IV)–Oxo Intermediates
2. Versatility of biological non-heme Fe(II) centers in oxygen activation reactions
3. Dioxygen Activation at Mononuclear Nonheme Iron Active Sites: Enzymes, Models, and Intermediates
4. High-Valent Iron(IV)–Oxo Complexes of Heme and Non-Heme Ligands in Oxygenation Reactions
5. The status of high-valent metal oxo complexes in the P450 cytochromes
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1. COST Action CM1201 “Biomimetic Radical Chemistry”: free radical chemistry successfully meets many disciplines;Free Radical Research;2016-11-01
2. Ligand-dependent oxidation of copper bound α-amino-isobutyric acid as 1-aminocyclopropane-1-carboxylic acid oxidase mimics;Polyhedron;2015-09
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