11.2: Bioinorganic Chemistry (Bertini et al.)
- Page ID
- 437980
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\(\newcommand{\avec}{\mathbf a}\) \(\newcommand{\bvec}{\mathbf b}\) \(\newcommand{\cvec}{\mathbf c}\) \(\newcommand{\dvec}{\mathbf d}\) \(\newcommand{\dtil}{\widetilde{\mathbf d}}\) \(\newcommand{\evec}{\mathbf e}\) \(\newcommand{\fvec}{\mathbf f}\) \(\newcommand{\nvec}{\mathbf n}\) \(\newcommand{\pvec}{\mathbf p}\) \(\newcommand{\qvec}{\mathbf q}\) \(\newcommand{\svec}{\mathbf s}\) \(\newcommand{\tvec}{\mathbf t}\) \(\newcommand{\uvec}{\mathbf u}\) \(\newcommand{\vvec}{\mathbf v}\) \(\newcommand{\wvec}{\mathbf w}\) \(\newcommand{\xvec}{\mathbf x}\) \(\newcommand{\yvec}{\mathbf y}\) \(\newcommand{\zvec}{\mathbf z}\) \(\newcommand{\rvec}{\mathbf r}\) \(\newcommand{\mvec}{\mathbf m}\) \(\newcommand{\zerovec}{\mathbf 0}\) \(\newcommand{\onevec}{\mathbf 1}\) \(\newcommand{\real}{\mathbb R}\) \(\newcommand{\twovec}[2]{\left[\begin{array}{r}#1 \\ #2 \end{array}\right]}\) \(\newcommand{\ctwovec}[2]{\left[\begin{array}{c}#1 \\ #2 \end{array}\right]}\) \(\newcommand{\threevec}[3]{\left[\begin{array}{r}#1 \\ #2 \\ #3 \end{array}\right]}\) \(\newcommand{\cthreevec}[3]{\left[\begin{array}{c}#1 \\ #2 \\ #3 \end{array}\right]}\) \(\newcommand{\fourvec}[4]{\left[\begin{array}{r}#1 \\ #2 \\ #3 \\ #4 \end{array}\right]}\) \(\newcommand{\cfourvec}[4]{\left[\begin{array}{c}#1 \\ #2 \\ #3 \\ #4 \end{array}\right]}\) \(\newcommand{\fivevec}[5]{\left[\begin{array}{r}#1 \\ #2 \\ #3 \\ #4 \\ #5 \\ \end{array}\right]}\) \(\newcommand{\cfivevec}[5]{\left[\begin{array}{c}#1 \\ #2 \\ #3 \\ #4 \\ #5 \\ \end{array}\right]}\) \(\newcommand{\mattwo}[4]{\left[\begin{array}{rr}#1 \amp #2 \\ #3 \amp #4 \\ \end{array}\right]}\) \(\newcommand{\laspan}[1]{\text{Span}\{#1\}}\) \(\newcommand{\bcal}{\cal B}\) \(\newcommand{\ccal}{\cal C}\) \(\newcommand{\scal}{\cal S}\) \(\newcommand{\wcal}{\cal W}\) \(\newcommand{\ecal}{\cal E}\) \(\newcommand{\coords}[2]{\left\{#1\right\}_{#2}}\) \(\newcommand{\gray}[1]{\color{gray}{#1}}\) \(\newcommand{\lgray}[1]{\color{lightgray}{#1}}\) \(\newcommand{\rank}{\operatorname{rank}}\) \(\newcommand{\row}{\text{Row}}\) \(\newcommand{\col}{\text{Col}}\) \(\renewcommand{\row}{\text{Row}}\) \(\newcommand{\nul}{\text{Nul}}\) \(\newcommand{\var}{\text{Var}}\) \(\newcommand{\corr}{\text{corr}}\) \(\newcommand{\len}[1]{\left|#1\right|}\) \(\newcommand{\bbar}{\overline{\bvec}}\) \(\newcommand{\bhat}{\widehat{\bvec}}\) \(\newcommand{\bperp}{\bvec^\perp}\) \(\newcommand{\xhat}{\widehat{\xvec}}\) \(\newcommand{\vhat}{\widehat{\vvec}}\) \(\newcommand{\uhat}{\widehat{\uvec}}\) \(\newcommand{\what}{\widehat{\wvec}}\) \(\newcommand{\Sighat}{\widehat{\Sigma}}\) \(\newcommand{\lt}{<}\) \(\newcommand{\gt}{>}\) \(\newcommand{\amp}{&}\) \(\definecolor{fillinmathshade}{gray}{0.9}\)This text covers material that could be included in a one-quarter or one-semester course in bioinorganic chemistry for graduate students and advanced undergraduate students in chemistry or biochemistry. The authors believe that such a course should provide students with the background required to follow the research literature in the field. The topics were chosen to represent those areas of bioinorganic chemistry that are mature enough for textbook presentation. Although each chapter presents material at a more advanced level than that of bioinorganic textbooks published previously, the chapters are not specialized review articles.
- 11.2.1: Transition-Metal Storage, Transport, and Biomineralization
- 11.2.1.1: Biological Significance of Iron, Zinc, Copper, Molybdenum, Cobalt, Chromium, Vanadium, and Nickel
- 11.2.1.2: Biological Systems of Metal Storage
- 11.2.1.3: Chemical Properties Relative to Storage and Transport
- 11.2.1.4: Iron Biomineralization
- 11.2.1.5: Transport of Iron
- 11.2.1.6: Transport of Zinc, Copper, Vanadium, Chromium, Molybdenum, and Cobalt
- 11.2.2: The Reaction Pathways of Zinc Enzymes and Related Biological Catalysts
- This chapter deals with metalloenzymes wherein the metal acts mainly as a Lewis acid; i.e., the metal does not change its oxidation state nor, generally, its protein ligands. Changes in the coordination sphere may occur on the side exposed to solvent. The substrate interacts with protein residues inside the active cavity and/or with the metal ion in order to be activated, so that the reaction can occur.
- 11.2.2.1: About Carbonic Anhydrase
- 11.2.2.2: Acid-base Equilibria
- 11.2.2.3: Catalytic Mechanism
- 11.2.2.4: Coordinated Water and NMR
- 11.2.2.5: Coordination Geometries
- 11.2.2.6: Ester Hydrolysis and Phosphoryl Transfer
- 11.2.2.7: Group Transfer and Vitamin B-12
- 11.2.2.8: Metal Substitution
- 11.2.2.9: Model Chemistry
- 11.2.2.10: Nucleophilic Addition of \(OH^{-}\) and \(H^{-}\)
- 11.2.2.11: Peptide Hydrolysis
- 11.2.2.12: pH Dependence of Inhibitor Binding
- 11.2.2.13: Selecting Zinc
- 11.2.2.14: Steady-State and Equilibrium Kinetics of Carbonic Anhydrase-Catalyzed \(CO_{2}/HCO_{3}^{-}\) Interconversion
- 11.2.2.15: Strategies for the Investigation of Zinc Enzymes
- 11.2.2.16: The Natural Catalysts
- 11.2.2.17: What Do We Learn?
- 11.2.3: Calcium in Biological Systems
- 11.2.3.1: Ca²⁺-binding Proteins in Microorganisms- The Search for a Prokaryotic Calmodulin
- 11.2.3.2: Basic Facts About Calcium- Its Compounds and Reactions
- 11.2.3.3: Calcium in Mineralized Tissues
- 11.2.3.4: Calmodulin
- 11.2.3.5: Extracellular Calcium Ion-binding Proteins
- 11.2.3.6: Inositol Trisphosphate and the Calcium Ion Messenger System
- 11.2.3.7: Intracellular Calcium Ion Transport
- 11.2.3.8: Measurements of "Free" Calcium Concentrations
- 11.2.3.9: Measurements of Total Calcium Concentrations
- 11.2.3.10: Mitochondrial Calcium Ion Transport
- 11.2.3.11: Molecular Aspects of Calcium Ion-Regulated Intracellular Processes (Part 1)
- 11.2.3.12: Molecular Aspects of Calcium Ion-regulated Intracellular Processes (Part 2)
- 11.2.3.13: Paravalbumin and Calbindins \(D_{9K}\) and \(D_{28K}\)
- 11.2.3.14: The Transport and Regulation of Ca²⁺ Ions in Higher Organisms
- 11.2.3.15: Troponin C
- 11.2.4: Biological and Synthetic Dioxygen Carriers
- 11.2.4.1: Biological Dioxygen Transport Systems
- 11.2.4.2: Biological Oxygen Carriers
- 11.2.4.3: Detailed Structures of Hemoglobins and Model Systems
- 11.2.4.4: Dioxygen Carriers and Bioinorganic Chemistry
- 11.2.4.5: General Aspects of the Chemistry of Cobalt
- 11.2.4.6: General Aspects of the Chemistry of Copper
- 11.2.4.7: General Aspects of the Chemistry of Dioxygen
- 11.2.4.8: General Aspects of the Chemistry of Iron
- 11.2.4.9: General Structural Features that Modulate Ligand Activity
- 11.2.4.10: Hazards of Life with Dioxygen
- 11.2.4.11: Nature of the Metal-Dioxygen Linkage in Biological Systems
- 11.2.4.12: Other Ligands for Biological Oxygen Carriers
- 11.2.4.13: Requirements for a Model System for Hemoglobin
- 11.2.4.14: Requirements for Effective Oxygen Carriers
- 11.2.4.15: Role of the Protein in Effecting Biological Oxygen Transport
- 11.2.4.16: Selected Chemistry of Dioxygen, Iron, Copper, and Cobalt
- 11.2.4.17: Stereochemical Changes Upon Ligation
- 11.2.4.18: Structural Basis of Ligand Affinities of Oxygen Carriers
- 11.2.4.19: Structures Relevant to Liganded Hemoglobins
- 11.2.4.20: Thermodynamic Factors
- 11.2.4.21: Ch. 4 References and Abbreviations
- 11.2.6: Electron Transfer
- 11.2.6.1: Biological Redox Components
- 11.2.6.2: Coupling Electron Transfers and Substrate Activation
- 11.2.6.3: Electron-transfer Rates
- 11.2.6.4: Electron-Transfer Theory
- 11.2.6.5: Energy Storage and Release
- 11.2.6.6: Long-range Electron Transfer in Proteins (Part 1)
- 11.2.6.7: Long-range Electron Transfer in Proteins (Part 2)
- 11.2.6.8: Marcus Theory
- 11.2.7: Ferrodoxins, Hydrogenases, and Nitrogenases - Metal-Sulfide Proteins
- 11.2.7.1: Iron-sulfur Proteins and Models
- 11.2.7.2: Iron-sulfur Proteins and Models (Part 2)
- 11.2.7.3: Iron-sulfur Proteins and Models (Part 3)
- 11.2.7.4: Iron-sulfur Proteins and Models (Part 4)
- 11.2.7.5: Multisite Redox Enzymes
- 11.2.7.6: Multisite Redox Enzymes (Part 2)
- 11.2.7.7: Multisite Redox Enzymes (Part 3)
- 11.2.7.8: Multisite Redox Enzymes (Part 4)
- 11.2.7.9: Multisite Redox Enzymes (Part 5)
- 11.2.7.10: Multisite Redox Enzymes (Part 6)
- 11.2.7.11: Report on the Nitrogenase Crystal Structure\(\;^{378-381}\)
- 11.2.7.12: Rubredoxin- A Single-Fe Tetrathiolate Protein
- 11.2.8: Metal/Nucleic Acid Interactions
- 11.2.8.1: The Basics
- 11.2.8.2: The Basics (Part 2)
- 11.2.8.3: A Case Study- Tris(phenanthroline) Metal Complexes
- 11.2.8.4: Applications of Different Metal Complexes that Bind Nucleic Acids
- 11.2.8.5: Applications of Different Metal Complexes that Bind Nucleic Acids (Part 2)
- 11.2.8.6: Nature's Use of Metal/Nucleic-acid Interactions
- 11.2.9: Metals in Medicine
- Metal ions are required for many critical functions in humans. Scarcity of some metal ions can lead to disease. Well-known examples include pernicious anemia resulting from iron deficiency, growth retardation arising from insufficient dietary zinc, and heart disease in infants owing to copper deficiency. The ability to recognize, to understand at the molecular level, and to treat diseases caused by inadequate metal-ion function constitutes an important aspect of medicinal bioinorganic chemistry.
- 11.2.9.1: Metal Deficiency and Disease
- 11.2.9.2: Toxic Effects of Metals
- 11.2.9.3: Aspects of Platinum Binding to DNA
- 11.2.9.4: Survey of Metals Used for Diagnosis and Chemotherapy
- 11.2.9.5: Platinum Anticancer Drugs- A Case Study
- 11.2.9.6: Mapping the Major Adducts of cis- and trans-DDP on DNA; Sequence Specificity
- 11.2.9.7: Structure of Platinum-DNA Complexes
- 11.2.9.8: Site-specifically Platinated DNA \(\;^{154}\)
- 11.2.9.9: Bioinorganic Chemistry of Platinum Anticancer Drugs- How Might They Work?
- 11.2.9.10: Bioinorganic Chemistry of Platinum Anticancer Drugs; How Might They Work? (Part 2)
- 11.2.9.11: Design of New Inorganic Anticancer Drugs
Thumbnail: The ball-and-stick model of diisobutylaluminium hydride, showing aluminium as pink, carbon as black, and hydrogen as white. Image used with permission (Public Domain; Benjah-bmm27).
Contributors and Attributions
Bertini, Ivano and Gray, Harry B. and Lippard, Stephen J. and Valentine, Joan Selverstone (1994) Bioinorganic Chemistry. University Science Books , Mill Valley, CA. ISBN 0-935702-57-1. http://resolver.caltech.edu/CaltechBOOK:1994.002