The oxo/peroxo debate: a nonheme iron perspective.
The oxygen activation mechanisms proposed for nonheme iron systems generally follow the heme paradigm in invoking the involvement of iron-peroxo and iron-oxo species in their catalytic cycles. However, the nonheme ligand environments allow for end-on and side-on dioxygen coordination and impart greater flexibility in the modes of dioxygen activation. The currently available evidence for nonheme iron-peroxo and iron-oxo intermediates is summarized and discussed in light of the ongoing discussion on the nature of the oxidant(s) in heme enzymes.
Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, Minneapolis, MN 55455, USA. que@chem.umn.edu
Lawrence
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Que
D001761:Bleomycin / Q000737:chemistry; D049308:Dioxygenases / Q000737:chemistry; D058085:Iron Compounds / Q000737:chemistry*; D007656:Ketoglutaric Acids / Q000737:chemistry; D008667:Metalloproteins / Q000737:chemistry; D006899:Mixed Function Oxygenases / Q000737:chemistry; D008968:Molecular Conformation; D015394:Molecular Structure; D009097:Multienzyme Complexes / Q000737:chemistry; D009942:Organometallic Compounds / Q000737:chemistry*; D016877:Oxidants / Q000737:chemistry; D010105:Oxygenases / Q000737:chemistry; D012264:Ribonucleotide Reductases / Q000737:chemistry
D058085:Iron Compounds; D007656:Ketoglutaric Acids; D008667:Metalloproteins; D009097:Multienzyme Complexes; D009942:Organometallic Compounds; D016877:Oxidants; D001761:Bleomycin; D006899:Mixed Function Oxygenases; D010105:Oxygenases; D049308:Dioxygenases; C433064:taurine-alpha-ketoglutarate dioxygenase; C038703:naphthalene dioxygenase; C021555:methane monooxygenase; D012264:Ribonucleotide Reductases