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TAKAFUMI UENO is Professor in the School and Graduate School of Bioscience and Biotechnology at Tokyo Institute of Technology. His current research interests involve the molecular design of artificial metalloproteins and exploitation of meso-scale materials with the coordination chemistry of protein assemblies. He was awarded the Young Investigator Award of the Japan Society of Coordination Chemistry in 2007 and the Young Scientists' Prize of the Commendation for Science and Technology by the Minister of Education, Culture, Sports, Science and Technology, Japan, in 2008.
YOSHIHITO WATANABE is Professor in the Department of Chemistry at Nagoya University. Since 2009, he has been appointed a Vice President of Research and International Affairs. His current research interests include the design of hydrogen peroxide-dependent monooxygenase and construction of metalloenzymes with synthetic complexes at their catalytic centers. He is a recipient of the Chemical Society of Japan Award for Creative Work in 1999, and the Japan Society of Coordination Chemistry in 2011. He sits on two editorial boards and an international advisory board.
Foreword
Harry B. Gray
Part 1. Coordination Chemistry in Native Protein Cages
1. The Chemistry of Nature’s Iron Biominerals in Ferritin Protein Nanocages
Elizabeth C. Theil and Rabindra K. Behera
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 Perspective
2. Molecular Metal Oxides in Protein Cages/Cavities
Achim Müller and Dieter Rehder
2.1 Introduction
2.2 Vanadium: Functional Oligovanadates and Storage of VO2+ in Vanabins
2.3 Molybdenum and Tungsten: Nucleation Processes 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
Part 2. Design of Metalloprotein Cages
3. De novo Design of Protein Cages to Accommodate metal cofactors
Flavia Nastri, Rosa Bruni, Ornella Maglio and Angela Lombardi
3.1 Introduction
3.2 De novo designed protein cages housing mono-nuclear metal cofactors
3.3 De novo designed protein cages housing di-nuclear metal cofactors.
3.4 De novo designed protein cages housing heme cofactors.
3.5 Conclusions and Perspectives
4. Generation of Functionalized Biomolecules Using Hemoprotein Matrices with Small Protein Cavities for Incorporation of Cofactors
Takashi Hayashi
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 peroixdase 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 Conclusion
5. Rational Design of Protein Cages for Alternative Enzymatic Functions
Nicolas Marshall, Kyle D. Miner, Tiffany D. Wilson and Yi Lu
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 (SOD)
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 Conclusions and Future Directions
Part 3. Coordination chemistry of protein assembly cages
6. Metal-Directed and Templated Assembly of Protein Superstructures and Cages
F. Akif Tezcan
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 Conclusion
7. Catalytic Reactions Proceeded in Protein Assembly Cages
Takafumi Ueno and Satoshi Abe
7.1 Introduction
7.1.1 Incorporation of metal compounds
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 reaction in ferritin
7.3.1 Olefin hydrogenation
7.3.2 Suzuki-Miyaura coupling
7.3.3 Polymer synthesis
7.4 Coordination process in ferritin
7.4.1 Metal ions
7.4.2 Metal complexes
7.4.3 Various coordination geometries designed in ferritin
7.5 Summary and Perspectives
8. Metal-Catalyzed Organic Transformations inside a Protein scaffold Using Artificial Metalloenzymes
V. K. K. Praneeth and Thomas R. Ward
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 Perspectives
Part 4. Applications in biology
9. Selective Labeling and Imaging of Protein Using Metal Complex
Yasutaka Kurishita and Itaru Hamachi
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 Conclusion
10. Molecular Bioengineering of Magnetosomes for Biotechnological Applications
Atsushi Arakaki, Michiko Nemoro and Tadashi Matsunaga
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 Concluding remarks
Part 5. Applications in nanotechnology
11. Protein Cage Nanoparticles for Hybrid Inorganic-Organic Materials
Shefah Qazi, Janice Lucon, Masaki Uchida and Trevor Douglas
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 Cages Nanoparticles (PCNs)
11.3.1 Introduction
11.3.2 Azide-Alkyne Click Chemistry (AACC) in sHsp and P22
11.3.3 Atom Transfer Radical Polymerization (ATRP) in P22
11.3.4 Application as Magnetic Resonance Imaging Contrast Agents (MRI-CAs)
11.4 Coordination Polymers in Protein Cages
11.4.1 Introduction
11.4.2 Metal-Organic Branched Polymer Synthesis by Pre-Forming 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 Conclusion
12. Nanoparticles Synthesized and Delivered by Protein in the Field of Nanotechnology Applications
Ichiro Yamashita, Kenji Iwahori, Bin Zheng, Shinya Kumagai
12.1.1 Nano particles (NPs) synthesis in a bio-template
12.1.1 NPs 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 NPs synthesis in the apoferritin with the metal binding peptides
12.2 Site-directed placement of NPs
12.2.1 Nano-positioning of cage-shaped proteins
12.2.2 Nano-positioning of 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
13. Engineered “Cages” for Design of Nanostructured Inorganic Materials
Patrick B. Dennis, Joseph M. Slocik and Rajesh R. Naik
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 Conclusion
Part 6. Coordination chemistry inspired by protein cages
14. Metal-organic Caged Assemblies
Sota Sato and Makoto Fujita
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
14.3.2 Chemistry on the periphery of cages
14.4 Toward a cage for a protein
14.5 Conclusion
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