title: Dioxygen-activating bio-inorganic model complexes.
abstract: The study of model compounds continues to significantly contribute to our understanding of the role of transition metals at the active sites of enzymes. Recent advances in the field include the use of mimics for enzymes that activate dioxygen, as dioxygen is not only manipulated in nature but also has industrial significance in metal-catalyzed oxidations of organics. Copper, nonheme and heme iron coordination complexes have been used to mimic reversible dioxygen-binding by the three classes of blood-oxygen carriers - hemocyanin, hemerythrin and hemoglobin/myoglobin - while functional mimics of oxygenases and oxidases with copper and iron have also provided key insights into important dioxygen activation processes.
authors.affiliation: Department of Chemistry, Remsen Hall, John Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.
authors.forename: H C
authors.initials: HC
authors.lastname: Liang
authors.forename: M
authors.initials: M
authors.lastname: Dahan
authors.forename: K D
authors.initials: KD
authors.lastname: Karlin
mesh_terms: D003300:Copper / Q000378:metabolism; D006422:Hemerythrin / Q000378:metabolism; D008956:Models, Chemical; D008958:Models, Molecular; D010088:Oxidoreductases / Q000378:metabolism; D010100:Oxygen / Q000378:metabolism*; D010105:Oxygenases / Q000378:metabolism
chemical_list: D006422:Hemerythrin; D003300:Copper; D010088:Oxidoreductases; D010105:Oxygenases; D010100:Oxygen