Bioinorganic chemistry of copper /
Karlin, Kenneth D.,1948-
Tyeklár, Zoltán.
Hopkins Copper Conference(1992 :Johns Hopkins University)
New York, N.Y. ; London : Chapman & Hall,
1993.
Based on papers presented at the Hopkins Copper Conference, held at John Hopkins University in Aug. 1992.
Includes bibliographical references and index.
Copper proteins and complex spectroscopy -- Electronic structures of active sites in copper proteins -- Pulsed EPR studies of copper proteins -- Copper(II) complexes of binucleating macrocyclic bid(disulfide) tetramine ligands -- Blue copper proteins and electron transfer -- Investigation of type 1 copper site geometry by spectroscopy and molecular redesign -- Metalloprotein ligand redesign -- Electron transfer reactivity of mutants of the blue copper protein plastocyanin -- Studies of CNI copper coordination compounds -- Natural and synthetic regulation of gene expression -- Chemical and genetic studies of copper resistance in E. coli -- Cuprous-thiolate polymetallic clusters in biology -- Mechanisms of copper ion homeostasis in yeast -- RNA hydrolysis by Cu(II) complexes.
(cont) Hemocyanin and copper monooxygenases -- Three-dimensional structure of the oxygenated form of the hemocyanin subunit II of Limulus polyphemus at atomic resolution -- New probes of oxygen binding and activation -- Chemical and spectroscopic studies on dopamine β-hydroxylase and other copper monooxygenases -- Copper ions in the membrane-associated methane monooxygenase -- Enzymology of peptide amidation -- Copper-mediated redox/oxidative pathways -- Redox decomposition reactions of copper(III) peptide complexes -- Free radical induced cleavage of organic molecules catalyzed by copper ions -- Copper-mediated nitrogen ligand oxidation and oxygenation -- Dioxygen-binding and oxygenation reactions -- Synthesis, structure and properties of u-n²:n² peroxo dinuclear copper complexes modeling the active site of oxyhemocyanin and oxytyrosinase -- Kinetics and mechanisms of Cu(I)/O₂ reactions -- Functional models for hemocyanin and copper monooxygenases.
(cont) Dioxygen activation by biomimetic dinuclear complexes -- Oxidation catalysis -- Dioxygen activation and transport by dinuclear copper(I) macrocyclic complexes -- Imidazole-ligated copper complexes -- Oxidation of unactivated hydrocarbons: models for tyrosinase and dopamine β-hydroxylase -- Copper-pteridine chemistry -- Design and synthesis of model systems for dioxygen binding and activation in dinuclear copper proteins -- Copper dioxygenation chemistry relevant to quercetin dioxygenase -- Nitrogen oxide (NOx) chemistry and biochemistry -- Two crystal forms of A. cycloclastes nitrite reductase -- Characterization of mononuclear copper-nitrogen oxide complexes: models of NOx binding to isolated active sites in copper proteins -- EPR-detectable copper of nitrous oxide reductase as a model for CuA in cytochrome c oxidase: a multifrequency electron paramagnetic resonance investigation.
(cont) Mixed-ligand, NON-nitrosyl Cu(II) complexes as potential pharmacological agents via NO release -- Copper oxidases -- Copper-containing enzymes: structure and mechanism -- Active site ligand interactions in galactose oxidase -- Structure and reactivity of copper-containing amine oxidases -- Ascorbate oxidase structure and chemistry -- Cytochrome c oxidase: a brief introduction and some new results from high field ENDOR studies of the CuA and CuB sites.
Copper