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Kategorie szczegółowe BISAC

Bioinorganic Chemistry of Copper

ISBN-13: 9789401168779 / Angielski / Miękka / 2013 / 506 str.

K. D. Karlin;Z. Tyeklar
Bioinorganic Chemistry of Copper K. D. Karlin                             Z. Tyeklar 9789401168779 Springer - książkaWidoczna okładka, to zdjęcie poglądowe, a rzeczywista szata graficzna może różnić się od prezentowanej.

Bioinorganic Chemistry of Copper

ISBN-13: 9789401168779 / Angielski / Miękka / 2013 / 506 str.

K. D. Karlin;Z. Tyeklar
cena 603,81
(netto: 575,06 VAT:  5%)

Najniższa cena z 30 dni: 578,30
Termin realizacji zamówienia:
ok. 16-18 dni roboczych.

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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.

Kategorie:
Nauka, Biologia i przyroda
Kategorie BISAC:
Science > Biochemia
Medical > Farmakologia
Science > Zoologia i nauki o zwierzętach
Wydawca:
Springer
Język:
Angielski
ISBN-13:
9789401168779
Rok wydania:
2013
Wydanie:
Softcover Repri
Ilość stron:
506
Waga:
0.77 kg
Wymiary:
22.9 x 15.2
Oprawa:
Miękka
Wolumenów:
01
Dodatkowe informacje:
Wydanie ilustrowane

Good bibliographies accompany each article. A book for the reference shelf of any laboratory group working with bioinorganic copper - Chemical Monographs Review; Summarizing the book may be a variable asset for those working or considering starting in biological copper research, as it gives a pretty complete review of current developments in the field - Molecular Biology Reports; This book provides an intriguing insight of current expertise in the Bioinorganic chemistry of copper - ioinorganic Chemistry of Copper; Good bibliographies accompany each article. A book for the reference shelf of any laboratory group working with bioinorganic copper - Chemical Monographs Review; Good bibliographies accompany each article. A book for the reference shelf of any laboratory group working with bioinorganic copper - Chemical Monographs Review

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

Kenneth D. Karlin is Ira Remsen Professor of Chemistry at Johns Hopkins University. His bioinorganic research focuses on coordination chemistry relevant to biological and environmental processes, involving copper or heme (porphyrin-iron) complexes. Dr. Karlin's main approach involves synthetic modeling, i.e., biomimetic chemistry. He is the winner of the prestigious F. Albert Cotton Award in Synthetic Inorganic Chemistry and the Sierra Nevada Distinguished Chemist Award, both awarded in 2009.



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