Bioinorganic chemistry of copper
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Bibliographic Information
Bioinorganic chemistry of copper
Chapman & Hall, 1993
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Note
Based on papers presented at the Hopkins Copper Conference, held at Johns Hopkins University in Aug. 1992
Includes bibliographical references and index
Description and Table of Contents
Description
"Bioinorganic Chemistry of Copper" focuses on the vital role of copper ions in biology, especially as an essential metalloenzyme cofactor. The book is interdisciplinary in its approach - the contributors includes co-ordination chemists, biochemists, biophysicists, and molecular biologists. Chapters are grouped into major areas of research interest in inorganic copper chemistry, spectroscopy, oxygen chemistry, biochemistry, and molecular biology. The book also discusses basic research of great potential importance to pharmaceutical scientists. This book is based on the first Johns Hopkins University Copper Symposium, held in August 1992. Researchers in chemistry, biochemistry, molecular biology, and medicinal chemistry should find it to be an essential reference on its subject. This book should be of interest to researchers in chemistry, biochemistry, molecular biology and medicinal chemistry.
Table of Contents
- Copper protein and complex spectroscopy - electronic structures of active sites in ccopper proteins, E.I. Solomon, et al
- pulsed EPR studies of copper proteins, J. Peisacch
- copper (II) complexes of binucleating macrocyclic bis(disulfide) tetramine ligands, S. Fox, et al
- blue'' copper proteins and electron transfer - investigation of type 1 copper site geometry by spectroscopy and molecular redesign, J. Sanders-Leohr
- metalloprotein ligand redesign - characterization of copper-cysteinate proteins derived from yeast copper-zinc superoxide dismutase, Y. Lu, et al
- electron transfer reactivity of mutants of the blue copper protein plastocyanin, A.G. Sykes, et al
- studies of CNI copper co-ordination compounds - what determines of the electron-transfer rate of the blue-copper proteins?, A. Flanagan, et al
- natural and synthetic regulation of gene expression - chemical and genetic studies of copper resistance in E. coli, J.W. Bryson, et al
- cuprous-thiolate polymetallic clusters in biology, D.R. Winge, et al
- mechanisms of copper ion homeostasis in yeast, V.C. Culotta, et al
- hydrolysis by Cu(II) complexes - toward synthetic ribonucleases and ribozymes, J.K. Bashkin
- hemocyanin and copper mono-oxygenases - three-dimensional structure of the oxygenated form of the hemocyanin subunit II of limulus polyphemus at atomic resolution, K.A. Magnus, et al
- new probes of oxygen binding and activiation - application to dopamine #B-mono-oxyenase, J. Klinman, et al
- chemical and spectroscopic studies on dopamine #B-hydroxylase and other copper mono-oxygenases, N.J. Blackburn
- the copper ions in the membrane-associated methane mono-oxygenase, S.I. Chan, et al
- the enzymology of peptide amidation, D.J. Merkler, et al
- copper-mediated redox/oxidative pathways - redox decomposition reactions of copper(III) peptide complexes, D.W. Margerum, et al
- free radicals induced cleavage of organic molecules catalyzed by copper ions - an alternative pathway for biological damage, S. Goldstein, et al
- copper-mediated nitrogen ligand oxidation and oxygenation, L.M. Sayre, et al
- 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.
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