Title:
Inorganic biochemistry : research progress
Publication Information:
New York : Nova Science Publishers, c2008
Physical Description:
xii, 345 p. : ill. (some col.) ; 26 cm.
ISBN:
9781604567083
Subject Term:
Available:*
Library | Item Barcode | Call Number | Material Type | Item Category 1 | Status |
---|---|---|---|---|---|
Searching... | 30000010236229 | QP531 I56 2008 | Open Access Book | Book | Searching... |
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Summary
Summary
Inorganic biochemistry is an emerging subject and interdisciplinary field between inorganic chemistry and biochemistry. The task of inorganic biochemistry is to research the interaction between the metal complex (or metal ion) with biological ligand at the molecular level. There exists wide research about inorganic biochemistry such as biological macromolecular, oxygen carrier, haemoglobin, mimic enzyme, DNA-binding and cytotoxicity, biological mineralisation, etc. Encompassing the varied and disparate roles of metal ions in biology, the field of bioinorganic chemistry has reached a certain level of maturity. This book provides leading research from around the globe in this field.
Table of Contents
Preface | p. vii |
Expert Commentary: Linear vs. Crosslinked Macromolecules as Supports for Biocatalyzed Transformations: Recent Developments | p. 1 |
Chapter 1 Chimeric Metallonucleases - Design, Realization and Applications | p. 11 |
Chapter 2 Role of Metal ion in Inorganic Biochemistry | p. 27 |
Chapter 3 Catalytic Activity of Iron and Manganese Porphyrins Modulated by Different Microenvironments: Interesting Devices for Nanotechnology | p. 63 |
Chapter 4 Metal Based Drug Design | p. 105 |
Chapter 5 Electrochemical Behavior of Flavonoids in the Presence of Metal Ions | p. 161 |
Chapter 6 Theoretical Study on FeOOH Formation and Role of H[subscript 2]O on Cu[subscript B] Site at Early Stage of O[subscript 2] Reduction in Cytochrome C Oxidase | p. 185 |
Chapter 7 The Axial Ligand Effect on Substrate Monoxygenation by the Oxo-iron Active Species of Heme Enzymes. How does Cytochrome C Peroxidase Compare to Cytochrome P450? | p. 197 |
Chapter 8 The Mechanism of Action of Di-heme Peroxidases: A Theoretical Study | p. 225 |
Chapter 9 Catalase activity of diMn[superscript III] Complexes with the [Mn subscript 2 ([mu]-O[subscript 2]C[subscript 2]H[subscript 3])([mu]-OL)([mu]-OX) superscript 3+] Core (L = Polydentate Ligand; X = CH[subscript 3] or OC[subscript 2]H[subscript 3]). Structural Features that Control Catalysis | p. 243 |
Chapter 10 Functional and Structural Mimics of Superoxide Dismutase Enzymes | p. 281 |
Chapter 11 From Synthesis to Antitumoral Activity of Platinum(II) and Platinum(IV) Complexes with Bis(carboxyalkylamino)ethane and -propane Ligands | p. 305 |
Index | p. 327 |