D.P. Kessissoglou (Hrsg.)

Bioinorganic Chemistry

An Inorganic Perspective of Life
Herausgegeben:Kessissoglou, D. P.

• Gebundenes Buch

Produktbeschreibung

Bioinorganic chemistry is primarily concerned with the role of metal atoms in biology and is a very active research field. However, even though such important structures of metalloenzymes are known, as the MoFeCo of nitrogenase, Cu or Mn superoxide dismutase and plastocyanin, the synthetic routes to the modelling of such centers remains a matter of acute scientific interest. Other metalloenzymes, such as the Mn center of the oxygen evolving complex of PSII, are still the focus of in-depth examination, both spectroscopic and structural. Another area of concern is the interaction between drugs and metals and metal ion antagonism. Understanding the chemistry of metal ions in biological systems will bring benefits in terms of understanding such problems as biomineralization and the production of advanced materials by micro-organisms.
The 29 contributions to Bioinorganic Chemistry: An Inorganic Perspective of Life give an excellent summary of the state of the art in this field, covering areas from the NMR of paramagnetic molecules to the use of lanthanide porphyrins in artificial batteries.

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Produktdetails

• Nato Science Series C: 459
• Verlag: Springer / Springer Netherlands
• Artikelnr. des Verlages: 978-0-7923-3380-7
• 1995.
• Seitenzahl: 442
• Erscheinungstermin: 28. Februar 1995
• Englisch
• Abmessung: 241mm x 160mm x 29mm
• Gewicht: 824g
• ISBN-13: 9780792333807
• ISBN-10: 0792333802
• Artikelnr.: 21348156

Inhaltsangabe

Metalloenzymes.- Methane Monooxygenase.- The Coordination Chemistry of Iron in Biological Transport and Storage; Iron Removal in Vivo.- Siderophore-Mediated Iron Transport in Microbes.- On the Mechanism of Epoxidation and Hydroxylation Catalyzed by Iron Porphyrins. Evidence for Non-Intersecting Reaction Pathways.- Self-Assembly, Catalysis and Electron Transfer with Metalloporphyrins in Phospholipid Membranes.- Mechanistic Studies on the Binuclear Fe Enzymes Ribonucleotide Reductase and Purple Acid Phosphatase.- Structure and Reactivity of the Blue Copper Proteins.- Copper-Zinc Superoxide Dismutase: Mechanistic and Biological Studies.- NMR of Paramagnetic Molecules: A Contribution to the Understanding of Enzymatic Mechanisms.- Magnetic and EPR Studies of Superoxide Dismutases (SOD): Electronic Structure of the Active Sites for the (Copper-Zinc)SOD, Its Cobalt Substituted Derivative and the Iron(III)SOD from E. Coli.- Mechanism of Action of Thiamin Enzymes. Role of Metal Ions.- Metal-DNA Interaction.- Platinum Anticancer Drugs.- NMR Spectroscopic Structure Determination of Metal Ion - Oligonucleotide Complexes - The Results of Sequence-Selective Binding Studies.- Metal Ion-Coordinating Properties in Solution of Purine-Nucleoside 5'-Monophosphates and Some Analogues.- Metal-Nucleobase Chemistry: Coordination, Reactivity, and Base Pairing.- DNA Cleavage by Cationic Metalloporphyrins.- The Role of Metal Ions in Biological Systems and Medicine.- The Interaction of Heavy Metal Ions with DNA.- Thermodynamics and Kinetics of Competing Redox Processes during DNA Cleavage: Reactivity-Based Selectivity.- Modeling Active Sites.- Mo/S Chemistry and Its Importance in Enzymatic Catalysis.- Use of de Novo Designed Peptides for the Study of Metalloproteins and Enzymes.- Modeling theChemistry and Properties of Multinuclear Manganese Enzymes.- Manganese-Proteins and -Enzymes and Relevant Trinuclear Synthetic Complexes.- Catalytic Oxidation of Pollutants by Ligninase Models Based on Metalloporphyrins and Metallophthalocyanines.- Nickel Coordination Chemistry with Oxothiolate Ligands and Its Relevance to Hydrogenase Enzymes.- Artificial Batteries with Lanthanide Porphyrins?.- Novel Transition Metal Heteropolymetalates and Derivatives: Structural Chemistry, Biological and Catalytic Relevance.- Purple Acid Phosphatases and Catechol Oxidase and Their Model Compounds. Crystal Structure Studies of Purple Acid Phosphatase from Red Kidney Beans.- Molybdenum-Copper Antagonism.