Department of Chemistry, University of Pannonia, H-8201 Veszprém, Hungary.
Dalton Trans. 2020 Feb 11;49(6):1742-1746. doi: 10.1039/c9dt04551a.
The reactivity of the previously reported peroxo-adduct [FeIII2(μ-O)(μ-1,2-O2)(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.
先前报道的过氧加合物 [FeIII2(μ-O)(μ-1,2-O2)(IndH)2(solv)2]2+（1）（IndH = 1,3-双(2-吡啶基亚氨基)异吲哚啉）的反应性已在亲核（例如，烷基和芳基烷基醛的去甲酰化）和亲电（例如，酚的氧化）反应中进行了研究，作为核酶（RNR-R2）和醛去甲酰化氧化酶（ADO）酶的模拟物。基于详细的动力学和机理研究，我们进一步证明了双功能亲核性过氧中间体对于双铁氧化还原酶的建议。
