Bioinorganic chemistry of copper

書誌事項

Bioinorganic chemistry of copper

edited by Kenneth D. Karlin, Zoltán Tyeklár

Springer-Science+Business Media, c1993

  • : softcover

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注記

"Originally published by Chapman & Hall, Inc. in 1993. Softcover reprint of the hardcover 1st edition 1993"--T.p. verso

Includes bibliographical references and index

内容説明・目次

内容説明

Bioinorganic Chemistry of Copper focuses on the vital role of copper ions in biology, especially as an essential metalloenzyme cofactor. The book is highly interdisciplinary in its approach--the outstanding list of contributors includes coordination 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 will find it to be an essential reference on its subject.

目次

  • Copper protein and complex spectroscopy: Electronic structures of active sites in copper proteins-- E. I. Solomon, B. L. Hemming and D. E. Root
  • Pulsed EPR studies of copper proteins-- J. Peisach
  • Copper (II) complexes of binucleating macrocyclic Bis(disulfide) tetramine ligands-- S. Fox, J. A. Potenza, S. Knapp and H. J. Schugar
  • 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, J. A. Roe, E. B. Gralla and J. S. Valentine
  • Electron transfer reactivity of mutants of the blue copper protein plastocyanin-- A. G. Sykes, P. Kyritsis, M. Nordling and S. Young
  • Studies of CNI copper coordination compounds: what determines the electron-transfer rate of the blue-copper proteins?-- S. Flanagan, J. A. Gonz'alez, J. E. Bradshaw, L. J. Wilson, D. M. Stanbury, K. J. Haller and W. R. Scheidt
  • Natural and synthetic regulation of gene expression: Chemical and genetic studies of copper resistance in E. coli--J. W. Bryson, T. V. O'Halloran, D. A. Rouch, N. L. Brown, J. Camakaris and B. T. O. Lee
  • Cuprous-thiolate polymetallic clusters in biology-- D. R. Winge, C. T. Dameron, G. N. George, I. J. Pickering and I. G. Dance
  • Mechanisms of copper ion homeostasis in yeast-- V. C. Culotta, P. Lapinskas and X. F. Liu
  • RNA Hydrolysis by Cu(II) complexes: toward synthetic ribonucleases and ribozymes-- J. K. Bashkin
  • Hemocyanin and copper monooxygenases: three-dimensional structure of the oxygenated form of the hemocyanin subunit II of limulus polyphemus at atomic resolution-- K. A. Magnus, H. Ton-That and J. E. Carpenter
  • New probes of oxygen binding and activiation: application to dopamine #B-monooxygenase-- J. P. Klinman, J. A. Berry and G. Tian
  • Chemical and spectroscopic studies on dopamine #B-hydroxylase and other copper monooxygenases-- N. J. Blackburn
  • The copper ions in the membrane-associated methane monooxygenase-- S. I. Chan, H.-H. Nguyen, A. K. Shiemke and M. E. Lidstrom
  • The enzymology of peptide amidation-- D. J. Merkler, R. Kulathila, S. D. Young, J. Freeman and J. J. Villafranca
  • Cooper-mediated redox/oxidative pathways: Redox decomposition reactions of copper(III) peptide complexes-- D. W. Margerum, W. M. Scheper, M. R. McDonald, F. C. Fredericks, L. Wang and H. D. Lee
  • Free radicals induced cleavage of organic molecules catalyzed by copper ions--an alternative pathway for biological damage-- S. Goldstein, G. Czapski, H. Cohen and D. Meyerstein
  • Cooper-mediated nitrogen ligand oxidation and oxygenation-- L M. Sayre, W. Tang, K. V. Reddy and D. Nadkarni
  • 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-- N. Kitajima
  • Kinetics and mechanisms of Cu(I)/O2 reactions-- A. D. Zuberbuhler
  • Functional models for hemocyanin and copper monooxygenases-- Z. Tyekl'ar and K. D. Karlin
  • Dioxygen activation by biomimetic dinuclear complexes-- L. Casella and M. Gullotti
  • Oxidation catalysis: a dinuclear approach-- B. L. Feringa
  • Dioxygen activation and transport by dinuclear copper(I) macrocyclic complexes-- A. E. Martell, R. Menif, P. M. Ngwenya and D. A. Rockliffe
  • Imidazole-ligated copper complexes: synthesis, structure, and reactivity-- T. N. Sorrell, M. L. Garrity, J. L. Richards, F. C. Pigge and W. E. Allen
  • Oxidation of unactivated hydrocarbons: models for tyrosinase and dopamine #B-hydroxylase-- M. R'eglier, E. Amad'ei, E. H. Alilou, F. Eydoux, M. Pierrot and B. Waegell
  • Copper-pteridine chemistry: structures, properties, and phenylalanine hydroxylase models-- O. Yamauchi, A. Odani, H. Masuda and Y. Funahashi
  • Design and synthesis of model systems fo

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詳細情報

  • NII書誌ID(NCID)
    BB2032315X
  • ISBN
    • 9789401168779
  • LCCN
    93012323
  • 出版国コード
    ne
  • タイトル言語コード
    eng
  • 本文言語コード
    eng
  • 出版地
    Dordrecht
  • ページ数/冊数
    xvi, 506 p.
  • 大きさ
    23 cm
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