Bioinorganic chemistry of copper / edited by Kenneth D. Karlin, Zoltán Tyeklár.

Other author Karlin, Kenneth D., 1948-
Other author Tyeklár, Zoltán.
Other author Hopkins Copper Conference (1992 : Johns Hopkins University)
Format Book
Publication InfoNew York : Chapman & Hall, 1993.
Descriptionxvi, 506 pages : illustrations ; 24 cm
Subjects

Contents 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.
Contents (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.
Contents (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.
Contents (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.
General noteBased on papers presented at the Hopkins Copper Conference, held at Johns Hopkins University in Aug. 1992.
Bibliography noteIncludes bibliographical references and index.
LCCN 93012323

Availability

Library Location Call Number Status Item Actions
Joyner General Stacks QP535.C9 B56 1993 ✔ Available Place Hold