title: Non-heme iron enzymes: contrasts to heme catalysis.
abstract: Non-heme iron enzymes catalyze a wide range of O(2) reactions, paralleling those of heme systems. Non-heme iron active sites are, however, much more difficult to study because they do not exhibit the intense spectral features characteristic of the porphyrin ligand. A spectroscopic methodology was developed that provides significant mechanistic insight into the reactivity of non-heme ferrous active sites. These studies reveal a general mechanistic strategy used by these enzymes and differences in substrate and cofactor interactions dependent on their requirement for activation by iron. Contributions to O(2) activation have been elucidated for non-heme relative to heme ligand sets, and major differences in reactivity are defined with respect to the heterolytic and homolytic cleavage of O-O bonds.
authors.affiliation: Department of Chemistry, Stanford University, Stanford, CA 94305, USA. edward.solomon@stanford.edu
authors.forename: Edward I
authors.initials: EI
authors.lastname: Solomon
authors.forename: Andrea
authors.initials: A
authors.lastname: Decker
authors.forename: Nicolai
authors.initials: N
authors.lastname: Lehnert
mesh_terms: D001665:Binding Sites; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D006418:Heme / Q000378:metabolism*; D006860:Hydrogen Bonding; D007501:Iron / Q000378:metabolism*; D008024:Ligands; D010651:Phenylalanine Hydroxylase / Q000737:chemistry / Q000378:metabolism; D011166:Porphyrins / Q000378:metabolism; D013816:Thermodynamics
chemical_list: D004798:Enzymes; D008024:Ligands; D011166:Porphyrins; D006418:Heme; D007501:Iron; D010651:Phenylalanine Hydroxylase