COORDINATION CHEMISTRY IN PROTEIN CAGES -- Contents -- Foreword -- Preface -- Contributors -- PART I COORDINATION CHEMISTRY IN NATIVE PROTEIN CAGES -- 1 The Chemistry of Nature's Iron Biominerals in Ferritin Protein Nanocages -- 1.1 Introduction -- 1.2 Ferritin Ion Channels and Ion Entry -- 1.2.1 Maxi- and Mini-Ferritin -- 1.2.2 Iron Entry -- 1.3 Ferritin Catalysis -- 1.3.1 Spectroscopic Characterization of μ-1,2 Peroxodiferric Intermediate (DFP) -- 1.3.2 Kinetics of DFP Formation and Decay -- 1.4 Protein-Based Ferritin Mineral Nucleation and Mineral Growth -- 1.5 Iron Exit -- 1.6 Synthetic Uses of Ferritin Protein Nanocages -- 1.6.1 Nanomaterials Synthesized in Ferritins -- 1.6.2 Ferritin Protein Cages in Metalloorganic Catalysis and Nanoelectronics -- 1.6.3 Imaging and Drug Delivery Agents Produced in Ferritins -- 1.7 Summary and Perspectives -- Acknowledgments -- References -- 2 Molecular Metal Oxides in Protein Cages/Cavities -- 2.1 Introduction -- 2.2 Vanadium: Functional Oligovanadates and Storage of VO2+ in Vanabins -- 2.3 Molybdenum and Tungsten: Nucleation Process in a Protein Cavity -- 2.4 Manganese in Photosystem II -- 2.5 Iron: Ferritins, DPS Proteins, Frataxins, and Magnetite -- 2.6 Some General Remarks: Oxides and Sulfides -- References -- PART II DESIGN OF METALLOPROTEIN CAGES -- 3 De Novo Design of Protein Cages to Accommodate Metal Cofactors -- 3.1 Introduction -- 3.2 De Novo-Designed Protein Cages Housing Mononuclear Metal Cofactors -- 3.3 De Novo-Designed Protein Cages Housing Dinuclear Metal Cofactors -- 3.4 De Novo-Designed Protein Cages Housing Heme Cofactor -- 3.5 Summary and Perspectives -- Acknowledgments -- References -- 4 Generation of Functionalized Biomolecules Using Hemoprotein Matrices with Small Protein Cavities for Incorporation of Cofactors -- 4.1 Introduction.

4.2 Hemoprotein Reconstitution with an Artificial Metal Complex -- 4.3 Modulation of the O2 Affinity of Myoglobin -- 4.4 Conversion of Myoglobin into Peroxidase -- 4.4.1 Construction of a Substrate-Binding Site Near the Heme Pocket -- 4.4.2 Replacement of Native Heme with Iron Porphyrinoid in Myoglobin -- 4.4.3 Other Systems Used in Enhancement of Peroxidase Activity of Myoglobin -- 4.5 Modulation of Peroxidase Activity of HRP -- 4.6 Myoglobin Reconstituted with a Schiff Base Metal Complex -- 4.7 A Reductase Model Using Reconstituted Myoglobin -- 4.7.1 Hydrogenation Catalyzed by Cobalt Myoglobin -- 4.7.2 A Model of Hydrogenase Using the Heme Pocket of Cytochrome c -- 4.8 Summary and Perspectives -- Acknowledgments -- References -- 5 Rational Design of Protein Cages for Alternative Enzymatic Functions -- 5.1 Introduction -- 5.2 Mononuclear Electron Transfer Cupredoxin Proteins -- 5.3 CuA Proteins -- 5.4 Catalytic Copper Proteins -- 5.4.1 Type 2 Red Copper Sites -- 5.4.2 Other T2 Copper Sites -- 5.4.3 Cu, Zn Superoxide Dismutase -- 5.4.4 Multicopper Oxygenases and Oxidases -- 5.5 Heme-Based Enzymes -- 5.5.1 Mb-Based Peroxidase and P450 Mimics -- 5.5.2 Mimicking Oxidases in Mb -- 5.5.3 Mimicking NOR Enzymes in Mb -- 5.5.4 Engineering Peroxidase Proteins -- 5.5.5 Engineering Cytochrome P450s -- 5.6 Non-Heme ET Proteins -- 5.7 Fe and Mn Superoxide Dismutase -- 5.8 Non-Heme Fe Catalysts -- 5.9 Zinc Proteins -- 5.10 Other Metalloproteins -- 5.10.1 Cobalt Proteins -- 5.10.2 Manganese Proteins -- 5.10.3 Molybdenum Proteins -- 5.10.4 Nickel Proteins -- 5.10.5 Uranyl Proteins -- 5.10.6 Vanadium Proteins -- 5.11 Summary and Perspectives -- References -- PART III COORDINATION CHEMISTRY OF PROTEIN ASSEMBLY CAGES -- 6 Metal-Directed and Templated Assembly of Protein Superstructures and Cages -- 6.1 Introduction -- 6.2 Metal-Directed Protein Self-Assembly.

6.2.1 Background -- 6.2.2 Design Considerations for Metal-Directed Protein Self-Assembly -- 6.2.3 Interfacing Non-Natural Chelates with MDPSA -- 6.2.4 Crystallographic Applications of Metal-Directed Protein Self-Assembly -- 6.3 Metal-Templated Interface Redesign -- 6.3.1 Background -- 6.3.2 Construction of a Zn-Selective Tetrameric Protein Complex Through MeTIR -- 6.3.3 Construction of a Zn-Selective Protein Dimerization Motif Through MeTIR -- 6.4 Summary and Perspectives -- Acknowledgments -- References -- 7 Catalytic Reactions Promoted in Protein Assembly Cages -- 7.1 Introduction -- 7.1.1 Incorporation of Metal Compounds -- 7.1.2 Insight into Accumulation Process of Metal Compounds -- 7.2 Ferritin as a Platform for Coordination Chemistry -- 7.3 Catalytic Reactions in Ferritin -- 7.3.1 Olefin Hydrogenation -- 7.3.2 Suzuki-Miyaura Coupling Reaction in Protein Cages -- 7.3.3 Polymer Synthesis in Protein Cages -- 7.4 Coordination Processes in Ferritin -- 7.4.1 Accumulation of Metal Ions -- 7.4.2 Accumulation of Metal Complexes -- 7.5 Coordination Arrangements in Designed Ferritin Cages -- 7.6 Summary and Perspectives -- Acknowledgments -- References -- 8 Metal-Catalyzed Organic Transformations Inside a Protein Scaffold Using Artificial Metalloenzymes -- 8.1 Introduction -- 8.2 Enantioselective Reduction Reactions Catalyzed by Artificial Metalloenzymes -- 8.2.1 Asymmetric Hydrogenation -- 8.2.2 Asymmetric Transfer Hydrogenation of Ketones -- 8.2.3 Artificial Transfer Hydrogenation of Cyclic Imines -- 8.3 Palladium-Catalyzed Allylic Alkylation -- 8.4 Oxidation Reaction Catalyzed by Artificial Metalloenzymes -- 8.4.1 Artificial Sulfoxidase -- 8.4.2 Asymmetric cis-Dihydroxylation -- 8.5 Summary and Perspectives -- References -- PART IV APPLICATIONS IN BIOLOGY -- 9 Selective Labeling and Imaging of Protein Using Metal Complex -- 9.1 Introduction.

9.2 Tag-Probe Pair Method Using Metal-Chelation System -- 9.2.1 Tetracysteine Motif/Arsenical Compounds Pair -- 9.2.2 Oligo-Histidine Tag/Ni(ii)-NTA Pair -- 9.2.3 Oligo-Aspartate Tag/Zn(ii)-DpaTyr Pair -- 9.2.4 Lanthanide-binding Tag -- 9.3 Summary and Perspectives -- References -- 10 Molecular Bioengineering of Magnetosomes for Biotechnological Applications -- 10.1 Introduction -- 10.2 Magnetite Biomineralization Mechanism in Magnetosome -- 10.2.1 Diversity of Magnetotactic Bacteria -- 10.2.2 Genome and Proteome Analyses of Magnetotactic Bacteria -- 10.2.3 Magnetosome Formation Mechanism -- 10.2.4 Morphological Control of Magnetite Crystal in Magnetosomes -- 10.3 Functional Design of Magnetosomes -- 10.3.1 Protein Display on Magnetosome by Gene Fusion Technique -- 10.3.2 Magnetosome Surface Modification by In Vitro System -- 10.3.3 Protein-mediated Morphological Control of Magnetite Particles -- 10.4 Application -- 10.4.1 Enzymatic Bioassays -- 10.4.2 Cell Separation -- 10.4.3 DNA Extraction -- 10.4.4 Bioremediation -- 10.5 Summary and Perspectives -- Acknowledgments -- References -- PART V APPLICATIONS IN NANOTECHNOLOGY -- 11 Protein Cage Nanoparticles for Hybrid Inorganic-Organic Materials -- 11.1 Introduction -- 11.2 Biomineral Formation in Protein Cage Architectures -- 11.2.1 Introduction -- 11.2.2 Mineralization -- 11.2.3 Model for Synthetic Nucleation-Driven Mineralization -- 11.2.4 Mineralization in Dps: A 12-Subunit Protein Cage -- 11.2.5 Icosahedral Protein Cages: Viruses -- 11.2.6 Nucleation of Inorganic Nanoparticles Within Icosahedral Viruses -- 11.3 Polymer Formation Inside Protein Cage Nanoparticles -- 11.3.1 Introduction -- 11.3.2 Azide-Alkyne Click Chemistry in sHsp and P22 -- 11.3.3 Atom Transfer Radical Polymerization in P22 -- 11.3.4 Application as Magnetic Resonance Imaging Contrast Agents.

11.4 Coordination Polymers in Protein Cages -- 11.4.1 Introduction -- 11.4.2 Metal-Organic Branched Polymer Synthesis by Preforming Complexes -- 11.4.3 Coordination Polymer Formation from Ditopic Ligands and Metal Ions -- 11.4.4 Altering Protein Dynamics by Coordination: Hsp-Phen-Fe -- 11.5 Summary and Perspectives -- Acknowledgments -- References -- 12 Nanoparticles Synthesized and Delivered by Protein in the Field of Nanotechnology Applications -- 12.1 Nanoparticle Synthesis in a Bio-Template -- 12.1.1 NP Synthesis by Cage-Shaped Proteins for Nanoelectronic Devices and Other Applications -- 12.1.2 Metal Oxide or Hydro-Oxide NP Synthesis in the Apoferritin Cavity -- 12.1.3 Compound Semiconductor NP Synthesis in the Apoferritin Cavity -- 12.1.4 NP Synthesis in the Apoferritin with the Metal-Binding Peptides -- 12.2 Site-Directed Placement of NPs -- 12.2.1 Nanopositioning of Cage-Shaped Proteins -- 12.2.2 Nanopositioning of Au NPs by Porter Proteins -- 12.3 Fabrication of Nanodevices by the NP and Protein Conjugates -- 12.3.1 Fabrication of Floating Nanodot Gate Memory -- 12.3.2 Fabrication of Single-Electron Transistor Using Ferritin -- References -- 13 Engineered "Cages" for Design of Nanostructured Inorganic Materials -- 13.1 Introduction -- 13.2 Metal-Binding Peptides -- 13.3 Discrete Protein Cages -- 13.4 Heat-Shock Proteins -- 13.5 Polymeric Protein and Carbohydrate Quasi-Cages -- 13.6 Summary and Perspectives -- References -- PART VI COORDINATION CHEMISTRY INSPIRED BY PROTEIN CAGES -- 14 Metal-Organic Caged Assemblies -- 14.1 Introduction -- 14.2 Construction of Polyhedral Skeletons by Coordination Bonds -- 14.2.1 Geometrical Effect on Products -- 14.2.2 Structural Extension Based on Rigid, Designable Framework -- 14.2.3 Mechanistic Insight into Self-Assembly -- 14.3 Development of Functions via Chemical Modification.

14.3.1 Chemistry in the Hollow of Cages.