Sets the stage for the design and application of new protein
cages

Featuring contributions from a team of international experts in
the coordination chemistry of biological systems, this book enables
readers to understand and take advantage of the fascinating
internal molecular environment of protein cages. With the aid of
modern organic and polymer techniques, the authors explain step by
step how to design and construct a variety of protein cages.
Moreover, the authors describe current applications of protein
cages, setting the foundation for the development of new
applications in biology, nanotechnology, synthetic chemistry, and
other disciplines.

Based on a thorough review of the literature as well as the
authors' own laboratory experience, Coordination Chemistry in
Protein Cages

* Sets forth the principles of coordination reactions in natural
protein cages

* Details the fundamental design of coordination sites of small
artificial metalloproteins as the basis for protein cage
design

* Describes the supramolecular design and assembly of protein
cages for or by metal coordination

* Examines the latest applications of protein cages in biology
and nanotechnology

* Describes the principles of coordination chemistry that govern
self-assembly of synthetic cage-like molecules

Chapters are filled with detailed figures to help readers
understand the complex structure, design, and application of
protein cages. Extensive references at the end of each chapter
serve as a gateway to important original research studies and
reviews in the field.

With its detailed review of basic principles, design, and
applications, Coordination Chemistry in Protein Cages is
recommended for investigators working in biological inorganic
chemistry, biological organic chemistry, and nanoscience.

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.

Sets the stage for the design and application of new protein cages

Featuring contributions from a team of international experts in the coordination chemistry of biological systems, this book enables readers to understand and take advantage of the fascinating internal molecular environment of protein cages. With the aid of modern organic and polymer techniques, the authors explain step by step how to design and construct a variety of protein cages. Moreover, the authors describe current applications of protein cages, setting the foundation for the development of new applications in biology, nanotechnology, synthetic chemistry, and other disciplines.

Based on a thorough review of the literature as well as the authors' own laboratory experience, Coordination Chemistry in Protein Cages

• Sets forth the principles of coordination reactions in natural protein cages
• Details the fundamental design of coordination sites of small artificial metalloproteins as the basis for protein cage design
• Describes the supramolecular design and assembly of protein cages for or by metal coordination
• Examines the latest applications of protein cages in biology and nanotechnology
• Describes the principles of coordination chemistry that govern self-assembly of synthetic cage-like molecules

Chapters are filled with detailed figures to help readers understand the complex structure, design, and application of protein cages. Extensive references at the end of each chapter serve as a gateway to important original research studies and reviews in the field.

With its detailed review of basic principles, design, and applications, Coordination Chemistry in Protein Cages is recommended for investigators working in biological inorganic chemistry, biological organic chemistry, and nanoscience.

Foreword xiii

Preface xv

Contributors xvii

PART I COORDINATION CHEMISTRY IN NATIVE PROTEIN CAGES

1 The Chemistry of Nature's Iron Biominerals in Ferritin Protein Nanocages 3
Elizabeth C. Theil and Rabindra K. Behera

1.1 Introduction 3

1.2 Ferritin Ion Channels and Ion Entry 6

1.2.1 Maxi- and Mini-Ferritin 6

1.2.2 Iron Entry 7

1.3 Ferritin Catalysis 8

1.3.1 Spectroscopic Characterization of -1,2 Peroxodiferric Intermediate (DFP) 8

1.3.2 Kinetics of DFP Formation and Decay 12

1.4 Protein-Based Ferritin Mineral Nucleation and Mineral Growth 13

1.5 Iron Exit 16

1.6 Synthetic Uses of Ferritin Protein Nanocages 17

1.6.1 Nanomaterials Synthesized in Ferritins 18

1.6.2 Ferritin Protein Cages in Metalloorganic Catalysis and Nanoelectronics 19

1.6.3 Imaging and Drug Delivery Agents Produced in Ferritins 19

1.7 Summary and Perspectives 20

Acknowledgments 20

References 21

2 Molecular Metal Oxides in Protein Cages/Cavities 25
Achim M¨uller and Dieter Rehder

2.1 Introduction 25

2.2 Vanadium: Functional Oligovanadates and Storage of VO2+ in Vanabins 26

2.3 Molybdenum and Tungsten: Nucleation Process in a Protein Cavity 28

2.4 Manganese in Photosystem II 33

2.5 Iron: Ferritins, DPS Proteins, Frataxins, and Magnetite 35

2.6 Some General Remarks: Oxides and Sulfides 38

References 38

PART II DESIGN OF METALLOPROTEIN CAGES

3 De Novo Design of Protein Cages to Accommodate Metal Cofactors 45
Flavia Nastri, Rosa Bruni, Ornella Maglio, and Angela Lombardi

3.1 Introduction 45

3.2 De Novo-Designed Protein Cages Housing Mononuclear Metal Cofactors 47

3.3 De Novo-Designed Protein Cages Housing Dinuclear Metal Cofactors 59

3.4 De Novo-Designed Protein Cages Housing Heme Cofactor 66

3.5 Summary and Perspectives 79

Acknowledgments 79

References 80

4 Generation of Functionalized Biomolecules Using Hemoprotein Matrices with Small Protein Cavities for Incorporation of Cofactors 87
Takashi Hayashi

4.1 Introduction 87

4.2 Hemoprotein Reconstitution with an Artificial Metal Complex 89

4.3 Modulation of the O2 Affinity of Myoglobin 90

4.4 Conversion of Myoglobin into Peroxidase 95

4.4.1 Construction of a Substrate-Binding Site Near the Heme Pocket 95

4.4.2 Replacement of Native Heme with Iron Porphyrinoid in Myoglobin 99

4.4.3 Other Systems Used in Enhancement of Peroxidase Activity of Myoglobin 100

4.5 Modulation of Peroxidase Activity of HRP 102

4.6 Myoglobin Reconstituted with a Schiff Base Metal Complex 103

4.7 A Re…