title: Spectroscopic and mechanistic studies of dinuclear metallohydrolases and their biomimetic complexes.
abstract: An enhanced understanding of the metal ion binding and active site structural features of phosphoesterases such as the glycerophosphodiesterase from Enterobacter aerogenes (GpdQ), and the organophosphate degrading agent from Agrobacterium radiobacter (OpdA) have important consequences for potential applications. Coupled with investigations of the metalloenzymes, programs of study to synthesise and characterise model complexes based on these metalloenzymes can add to our understanding of structure and function of the enzymes themselves. This review summarises some of our work and illustrates the significance and contributions of model studies to knowledge in the area.
authors.affiliation: School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia. gahan@uq.edu.au.
authors.forename: Lena J
authors.initials: LJ
authors.lastname: Daumann
authors.forename: Gerhard
authors.initials: G
authors.lastname: Schenk
authors.forename: David L
authors.initials: DL
authors.lastname: Ollis
authors.forename: Lawrence R
authors.initials: LR
authors.lastname: Gahan
mesh_terms: D016960:Agrobacterium tumefaciens / Q000201:enzymology; D001672:Biocompatible Materials / Q000138:chemical synthesis / Q000378:metabolism*; D020134:Catalytic Domain; D056831:Coordination Complexes / Q000138:chemical synthesis / Q000378:metabolism; D021902:Enterobacter aerogenes / Q000201:enzymology; D008670:Metals / Q000737:chemistry / Q000378:metabolism; D010755:Organophosphates / Q000737:chemistry / Q000378:metabolism; D010727:Phosphoric Diester Hydrolases / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D001672:Biocompatible Materials; D056831:Coordination Complexes; D008670:Metals; D010755:Organophosphates; D010727:Phosphoric Diester Hydrolases