Functional models of nonheme diiron enzymes: reactivity of the μ-oxo-μ-1,2-peroxo-diiron(iii) intermediate in electrophilic and nucleophilic reactions
Author:
Affiliation:
1. Department of Chemistry
2. University of Pannonia
3. H-8201 Veszprém
4. Hungary
Abstract
The ambiphilic behavior (electrophilic versus nucleophilic character) of the peroxo-diferric complex and its relative reactivity towards aldehydes and phenols have been discussed.
Funder
Hungarian Scientific Research Fund
Publisher
Royal Society of Chemistry (RSC)
Subject
Inorganic Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2020/DT/C9DT04551A
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1. Ribonucleotide Reductases
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4. Human deoxyhypusine hydroxylase, an enzyme involved in regulating cell growth, activates O2 with a nonheme diiron center
5. The Post-Translational Synthesis of a Polyamine-Derived Amino Acid, Hypusine, in the Eukaryotic Translation Initiation Factor 5A (eIF5A)
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