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.
Que
Lawrence
L
Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, Minneapolis, MN 55455, USA. que@chem.umn.edu
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