Journal
DALTON TRANSACTIONS
Volume 49, Issue 6, Pages 1742-1746Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c9dt04551a
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Funding
- Hungarian National Research Fund (OTKA) [K108489, GINOP-2.3.2-15-2016-00049]
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The reactivity of the previously reported peroxo-adduct [FeIII2(mu-O)(mu-1,2-O-2)(IndH)(2)(solv)(2)](2+) (1) (IndH = 1,3-bis(2-pyridyl-imino)isoindoline) has been investigated in nucleophilic (e.g., deformylation of alkyl and aryl alkyl aldehydes) and electrophilic (e.g. oxidation of phenols) stoichiometric reactions as biomimics of ribonucleotide reductase (RNR-R2) and aldehyde deformylating oxygenase (ADO) enzymes. Based on detailed kinetic and mechanistic studies, we have found further evidence for the ambiphilic behaviour of the peroxo intermediates proposed for diferric oxidoreductase enzymes.
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