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A growing family of O2 activating dinuclear iron enzymes with key catalytic diiron(III)-peroxo intermediates: Biological systems and chemical models

“…The diversity of those enzymes and the reactions they perform make them an important field of research not only in biochemistry but also in chemistry, notably for the development of environmentally friendly oxidation catalysts. Among diiron oxygenases, the methane mooxygenase is probably the enzyme that has been studied the most [1][2][3][4]. However, other diiron oxygenases, such as toluene monooxygenases [5], stearoyl-ACP Δ 9 desaturase [6][7][8] or ribonucleotide reductase [9], have been well studied, and their mechanisms have been well investigated [10].…”

Tuning acid–base cooperativity to create next generation silica-supported organocatalysts

“…To achieve this increased performance, catalyst designers have often looked to enzymatic systems as a source of inspiration. Enzymes employ several concepts to achieve high activity under relatively mild conditions, including hydrophobic binding pockets [2], well-defined metallic clusters as redox active sites [3], and cooperative interactions of different types of sites (e.g., ligand and metal cooperativity) [4][5][6]. These design features created by the complex polypeptide architecture can be further modified for other catalytic purposes through incorporation of non-natural metal complexes near the active site (i.e., artificial metalloenzymes) [7,8].…”

Carboxylate-bridged dinuclear manganese systems – From catalases to oxidation catalysis

“…Importantly, the catalytic activity of these enzymes does not involve loss or partial dissociation of the carboxylate bridge, although in other dinuclear manganese or iron enzymes a carboxylate shift has been found to play an important role in enzyme function (e.g. MMO) [27,28].…”