title: Protein crystal structures with ferrocene and ruthenocene-based enzyme inhibitors.
abstract: We have determined the protein X-ray crystal structures of four organometallic inhibitors in complex with their target enzyme carbonic anhydrase II. The barrel-shaped hydrophobic ferrocene and ruthenocene moieties have provided a structure-based avenue to better occupy the hydrophobic binding patch within the enzyme active site.
authors.affiliation: Eskitis Institute for Cell and Molecular Therapies, Griffith University, Nathan, Queensland 4111, Australia.
authors.forename: Adam J
authors.initials: AJ
authors.lastname: Salmon
authors.forename: Michael L
authors.initials: ML
authors.lastname: Williams
authors.forename: Andreas
authors.initials: A
authors.lastname: Hofmann
authors.forename: Sally-Ann
authors.initials: SA
authors.lastname: Poulsen
mesh_terms: D001665:Binding Sites; D024402:Carbonic Anhydrase II / Q000037:antagonists & inhibitors* / Q000378:metabolism; D002257:Carbonic Anhydrase Inhibitors / Q000737:chemistry*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D005296:Ferrous Compounds / Q000737:chemistry*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D000075163:Metallocenes; D009942:Organometallic Compounds / Q000737:chemistry*
chemical_list: D002257:Carbonic Anhydrase Inhibitors; D005296:Ferrous Compounds; D000075163:Metallocenes; D009942:Organometallic Compounds; C016721:ruthenocene; D024402:Carbonic Anhydrase II; C004998:ferrocene