{"product_id":"enzymatic-fuel-cells-from-fundamentals-to-applications-9781118369234","title":"Enzymatic Fuel Cells  From Fundamentals to","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003eCovering the fundamentals of enzymatic fuel cells as well as their design, optimization, integration, and future trends,   Enzymatic Fuel Cells provides practical applications of enzymatic fuel cells, including their use in biomedical applications and as power supplies for small portable power devices.\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003e\u003cp\u003e\u003ci\u003ePreface xv\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003ci\u003eContributors xvii\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 Introduction 1\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eHeather R. Luckarift, Plamen Atanassov, and Glenn R. Johnson\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 3\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Electrochemical Evaluation of Enzymatic Fuel Cells and Figures of Merit 4\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eShelley D. Minteer, Heather R. Luckarift, and Plamen Atanassov\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2.1 Introduction, 4\u003c\/p\u003e \u003cp\u003e2.2 Electrochemical Characterization, 5\u003c\/p\u003e \u003cp\u003e2.2.1 Open-Circuit Measurements, 5\u003c\/p\u003e \u003cp\u003e2.2.2 Cyclic Voltammetry, 5\u003c\/p\u003e \u003cp\u003e2.2.3 Electron Transfer, 6\u003c\/p\u003e \u003cp\u003e2.2.4 Polarization Curves, 6\u003c\/p\u003e \u003cp\u003e2.2.5 Power Curves, 8\u003c\/p\u003e \u003cp\u003e2.2.6 Electrochemical Impedance Spectroscopy, 8\u003c\/p\u003e \u003cp\u003e2.2.7 Multienzyme Cascades, 8\u003c\/p\u003e \u003cp\u003e2.2.8 Rotating Disk Electrode Voltammetry, 9\u003c\/p\u003e \u003cp\u003e2.3 Outlook, 9\u003c\/p\u003e \u003cp\u003eAcknowledgment, 10\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 10\u003c\/p\u003e \u003cp\u003eReferences, 10\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Direct Bioelectrocatalysis: Oxygen Reduction for Biological Fuel Cells 12\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eDmitri M. Ivnitski, Plamen Atanassov, and Heather R. Luckarift\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.1 Introduction, 12\u003c\/p\u003e \u003cp\u003e3.2 Mechanistic Studies of Intramolecular Electron Transfer, 13\u003c\/p\u003e \u003cp\u003e3.2.1 Determining the Redox Potential of MCO, 13\u003c\/p\u003e \u003cp\u003e3.2.2 Effect ofpHand Inhibitors on the Electrochemistry ofMCO, 17\u003c\/p\u003e \u003cp\u003e3.3 Achieving DET of MCO by Rational Design, 18\u003c\/p\u003e \u003cp\u003e3.3.1 Surface Analysis of Enzyme-Modified Electrodes, 20\u003c\/p\u003e \u003cp\u003e3.3.2 Design of MCO-Modified Biocathodes Based on Direct Bioelectrocatalysis, 21\u003cbr\u003e \u003cbr\u003e 3.3.3 Design of MCO-Modified “Air-Breathing” Biocathodes, 22\u003c\/p\u003e \u003cp\u003e3.4 Outlook, 25\u003c\/p\u003e \u003cp\u003eAcknowledgments, 26\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 26\u003c\/p\u003e \u003cp\u003eReferences, 27\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Anodic Catalysts for Oxidation of Carbon-Containing Fuels 33\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eRosalba A. Rincón, Carolin Lau, Plamen Atanassov, and Heather R. Luckarift\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4.1 Introduction, 33\u003c\/p\u003e \u003cp\u003e4.2 Oxidases, 34\u003c\/p\u003e \u003cp\u003e4.2.1 Electron Transfer Mechanisms of Glucose Oxidase, 34\u003c\/p\u003e \u003cp\u003e4.3 Dehydrogenases, 35\u003c\/p\u003e \u003cp\u003e4.3.1 The NADH Reoxidation Issue, 35\u003c\/p\u003e \u003cp\u003e4.3.2 Mediators for Electrochemical Oxidation of NADH, 37\u003c\/p\u003e \u003cp\u003e4.3.3 Electropolymerization of Azines, 38\u003c\/p\u003e \u003cp\u003e4.3.4 Alcohol Dehydrogenase as a Model System, 41\u003c\/p\u003e \u003cp\u003e4.4 PQQ-Dependent Enzymes, 42\u003c\/p\u003e \u003cp\u003e4.5 Outlook, 44\u003c\/p\u003e \u003cp\u003eAcknowledgment, 45\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 45\u003c\/p\u003e \u003cp\u003eReferences, 45\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Anodic Bioelectrocatalysis: From Metabolic Pathways to Metabolons 53\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eShuai Xu, Lindsey N. Pelster, Michelle Rasmussen, and Shelley D. Minteer\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5.1 Introduction, 53\u003c\/p\u003e \u003cp\u003e5.2 Biological Fuels, 53\u003c\/p\u003e \u003cp\u003e5.3 Promiscuous Enzymes Versus Multienzyme Cascades Versus Metabolons, 55\u003c\/p\u003e \u003cp\u003e5.3.1 Promiscuous Enzymes, 55\u003c\/p\u003e \u003cp\u003e5.3.2 Multienzyme Cascades, 56\u003c\/p\u003e \u003cp\u003e5.3.3 Metabolons, 56\u003c\/p\u003e \u003cp\u003e5.4 Direct and Mediated Electron Transfer, 57\u003c\/p\u003e \u003cp\u003e5.5 Fuels, 58\u003c\/p\u003e \u003cp\u003e5.5.1 Hydrogen, 58\u003c\/p\u003e \u003cp\u003e5.5.2 Ethanol, 58\u003c\/p\u003e \u003cp\u003e5.5.3 Methanol, 60\u003c\/p\u003e \u003cp\u003e5.5.4 Methane, 61\u003c\/p\u003e \u003cp\u003e5.5.5 Glucose, 61\u003c\/p\u003e \u003cp\u003e5.5.6 Sucrose, 65\u003c\/p\u003e \u003cp\u003e5.5.7 Trehalose, 65\u003c\/p\u003e \u003cp\u003e5.5.8 Fructose, 67\u003c\/p\u003e \u003cp\u003e5.5.9 Lactose, 68\u003c\/p\u003e \u003cp\u003e5.5.10 Lactate, 68\u003c\/p\u003e \u003cp\u003e5.5.11 Pyruvate, 69\u003c\/p\u003e \u003cp\u003e5.5.12 Glycerol, 70\u003c\/p\u003e \u003cp\u003e5.5.13 Fatty Acids, 70\u003c\/p\u003e \u003cp\u003e5.6 Outlook, 72\u003c\/p\u003e \u003cp\u003eAcknowledgment, 72\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 73\u003c\/p\u003e \u003cp\u003eReferences, 73\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Bioelectrocatalysis of Hydrogen Oxidation\/Reduction by Hydrogenases 80\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eAnne K. Jones, Arnab Dutta, Patrick Kwan, Chelsea L. McIntosh, Souvik Roy, and Sijie Yang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.1 Introduction, 80\u003c\/p\u003e \u003cp\u003e6.2 Hydrogenases, 81\u003c\/p\u003e \u003cp\u003e6.3 Biological Fuel Cells Using Hydrogenases: Electrocatalysis, 85\u003c\/p\u003e \u003cp\u003e6.4 Electrocatalysis by Functional Mimics of Hydrogenases, 92\u003c\/p\u003e \u003cp\u003e6.4.1 [FeFe]-Hydrogenase Models, 92\u003c\/p\u003e \u003cp\u003e6.4.2 [NiFe]-Hydrogenase Models, 95\u003c\/p\u003e \u003cp\u003e6.4.3 Incorporation of Outer Coordination Sphere Features, 97\u003c\/p\u003e \u003cp\u003e6.5 Outlook, 97\u003c\/p\u003e \u003cp\u003eAcknowledgments, 98\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 98\u003c\/p\u003e \u003cp\u003eReferences, 99\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Protein Engineering for Enzymatic Fuel Cells 109\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eElliot Campbell and Scott Banta\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7.1 Engineering Enzymes for Catalysis, 109\u003c\/p\u003e \u003cp\u003e7.2 Engineering Other Properties of Enzymes, 112\u003c\/p\u003e \u003cp\u003e7.2.1 Stability, 112\u003c\/p\u003e \u003cp\u003e7.2.2 Size, 113\u003c\/p\u003e \u003cp\u003e7.2.3 Cofactor Specificity, 113\u003c\/p\u003e \u003cp\u003e7.3 Enzyme Immobilization and Self-Assembly, 115\u003c\/p\u003e \u003cp\u003e7.3.1 Engineering for Supermolecular Assembly, 116\u003c\/p\u003e \u003cp\u003e7.4 Artificial Metabolons, 117\u003c\/p\u003e \u003cp\u003e7.4.1 DNA-Templated Metabolons, 117\u003c\/p\u003e \u003cp\u003e7.5 Outlook, 118\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 118\u003c\/p\u003e \u003cp\u003eReferences, 118\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Purification and Characterization of Multicopper Oxidases for Enzyme Electrodes 123\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eD. Matthew Eby and Glenn R. Johnson\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8.1 Introduction, 123\u003c\/p\u003e \u003cp\u003e8.2 General Considerations for MCO Expression and Purification, 124\u003c\/p\u003e \u003cp\u003e8.3 MCO Production and Expression Systems, 125\u003c\/p\u003e \u003cp\u003e8.4 MCO Purification, 128\u003c\/p\u003e \u003cp\u003e8.5 Copper Stability and Specific Considerations for MCO Production, 133\u003c\/p\u003e \u003cp\u003e8.6 Spectroscopic Monitoring and Characterization of Copper Centers, 136\u003c\/p\u003e \u003cp\u003e8.7 Outlook, 139\u003c\/p\u003e \u003cp\u003eAcknowledgment, 140\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 140\u003c\/p\u003e \u003cp\u003eReferences, 140\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Mediated Enzyme Electrodes 146\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eJoshua W. Gallaway\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9.1 Introduction, 146\u003c\/p\u003e \u003cp\u003e9.2 Fundamentals, 147\u003c\/p\u003e \u003cp\u003e9.2.1 Electron Transfer Overpotentials, 147\u003c\/p\u003e \u003cp\u003e9.2.2 Electron Transfer Rate, 151\u003c\/p\u003e \u003cp\u003e9.2.3 Enzyme Kinetics, 151\u003c\/p\u003e \u003cp\u003e9.3 Types of Mediation, 152\u003c\/p\u003e \u003cp\u003e9.3.1 Freely Diffusing Mediator in Solution, 152\u003c\/p\u003e \u003cp\u003e9.3.2 Mediation in Cross-Linked Redox Polymers, 154\u003c\/p\u003e \u003cp\u003e9.3.3 Further Redox Polymer Mediation, 156\u003c\/p\u003e \u003cp\u003e9.3.4 Mediation in Other Immobilized Layers, 160\u003c\/p\u003e \u003cp\u003e9.4 Aspects of Mediator Design I: Mediator Overpotentials, 162\u003c\/p\u003e \u003cp\u003e9.4.1 Considering Species Potentials in a Methanol–Oxygen BFC, 162\u003c\/p\u003e \u003cp\u003e9.4.2 The Earliest Methanol-Oxidizing BFC Anodes, 162\u003c\/p\u003e \u003cp\u003e9.4.3 A Four-Enzyme Methanol-Oxidizing Anode, 164\u003c\/p\u003e \u003cp\u003e9.5 Aspects of Mediator Design II: Saturated Mediator Kinetics, 165\u003c\/p\u003e \u003cp\u003e9.5.1 An Immobilized Laccase Cathode, 166\u003c\/p\u003e \u003cp\u003e9.5.2 Potential of the Osmium Redox Polymer, 167\u003c\/p\u003e \u003cp\u003e9.5.3 Concentration of Redox Sites in the Mediator Film, 170\u003c\/p\u003e \u003cp\u003e9.6 Outlook, 172\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 172\u003c\/p\u003e \u003cp\u003eReferences, 172\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Hierarchical Materials Architectures for Enzymatic Fuel Cells 181\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eGuinevere Strack and Glenn R. Johnson\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10.1 Introduction, 181\u003c\/p\u003e \u003cp\u003e10.2 Carbon Nanomaterials and the Construction of the Bio–Nano Interface, 184\u003c\/p\u003e \u003cp\u003e10.2.1 Carbon Black Nanomaterials, 184\u003c\/p\u003e \u003cp\u003e10.2.2 Carbon Nanotubes, 185\u003c\/p\u003e \u003cp\u003e10.2.3 Graphene, 187\u003c\/p\u003e \u003cp\u003e10.2.4 CNT-Decorated Porous Carbon Architectures, 188\u003c\/p\u003e \u003cp\u003e10.2.5 Buckypaper, 188\u003c\/p\u003e \u003cp\u003e10.3 Biotemplating: The Assembly of Nanostructured Biological–Inorganic Materials, 191\u003c\/p\u003e \u003cp\u003e10.3.1 Protein-Mediated 3D Biotemplating, 192\u003c\/p\u003e \u003cp\u003e10.4 Fabrication of Hierarchically Ordered 3D Materials for Enzyme and Microbial Electrodes, 194\u003c\/p\u003e \u003cp\u003e10.4.1 Chitosan–CNT Conductive Porous Scaffolds, 195\u003c\/p\u003e \u003cp\u003e10.4.2 Polymer\/Carbon Architectures Fabricated Using Solid Templates, 196\u003c\/p\u003e \u003cp\u003e10.5 Incorporating Conductive Polymers into Bioelectrodes for Fuel Cell Applications, 198\u003c\/p\u003e \u003cp\u003e10.5.1 Conductive Polymer-Facilitated DET Between Laccase and a Conductive Surface, 198\u003c\/p\u003e \u003cp\u003e10.5.2 Materials Design for MFC, 200\u003c\/p\u003e \u003cp\u003e10.6 Outlook, 201\u003c\/p\u003e \u003cp\u003eAcknowledgment, 201\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 201\u003c\/p\u003e \u003cp\u003eReferences, 202\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Enzyme Immobilization for Biological Fuel Cell Applications 208\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eLorena Betancor and Heather R. Luckarift\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e11.1 Introduction, 208\u003c\/p\u003e \u003cp\u003e11.2 Immobilization by Physical Methods, 209\u003c\/p\u003e \u003cp\u003e11.2.1 Adsorption, 209\u003c\/p\u003e \u003cp\u003e11.3 Entrapment as a Pre- and Post-Immobilization Strategy, 211\u003c\/p\u003e \u003cp\u003e11.3.1 Stabilization via Encapsulation, 212\u003c\/p\u003e \u003cp\u003e11.3.2 Redox Hydrogels, 212\u003c\/p\u003e \u003cp\u003e11.4 Enzyme Immobilization via Chemical Methods, 213\u003c\/p\u003e \u003cp\u003e11.4.1 Covalent Immobilization, 213\u003c\/p\u003e \u003cp\u003e11.4.2 Molecular Tethering, 213\u003c\/p\u003e \u003cp\u003e11.4.3 Self-Assembly, 215\u003c\/p\u003e \u003cp\u003e11.5 Orientation Matters, 216\u003c\/p\u003e \u003cp\u003e11.6 Outlook, 218\u003c\/p\u003e \u003cp\u003eAcknowledgment, 219\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 219\u003c\/p\u003e \u003cp\u003eReferences, 219\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 Interrogating Immobilized Enzymes in Hierarchical Structures 225\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eMichael J. Cooney and Heather R. Luckarift\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e12.1 Introduction, 225\u003c\/p\u003e \u003cp\u003e12.2 Estimating the Bound Active (Redox) Enzyme, 227\u003c\/p\u003e \u003cp\u003e12.2.1 Modeling the Performance of Immobilized Redox Enzymes in Flow-Through Mode to Estimate the Concentration of Substrate at the Enzyme Surface, 229\u003c\/p\u003e \u003cp\u003e12.3 Probing the Distribution of Immobilized Enzyme Within Hierarchical Structures, 232\u003c\/p\u003e \u003cp\u003e12.4 Probing the Immediate Chemical Microenvironments of Enzymes in Hierarchical Structures, 235\u003c\/p\u003e \u003cp\u003e12.5 Enzyme Aggregation in a Hierarchical Structure, 236\u003c\/p\u003e \u003cp\u003e12.6 Outlook, 238\u003c\/p\u003e \u003cp\u003eAcknowledgment, 239\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 239\u003c\/p\u003e \u003cp\u003eReferences, 239\u003c\/p\u003e \u003cp\u003e\u003cb\u003e13 Imaging and Characterization of the Bio–Nano Interface 242\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eKaren E. Farrington, Heather R. Luckarift, D. Matthew Eby, and Kateryna Artyushkova\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e13.1 Introduction, 242\u003c\/p\u003e \u003cp\u003e13.2 Imaging the Bio–Nano Interface, 243\u003c\/p\u003e \u003cp\u003e13.2.1 Scanning Electron Microscopy, 243\u003c\/p\u003e \u003cp\u003e13.2.2 Transmission Electron Microscopy, 248\u003c\/p\u003e \u003cp\u003e13.3 Characterizing the Bio–Nano Interface, 248\u003c\/p\u003e \u003cp\u003e13.3.1 X-Ray Photoelectron Spectroscopy, 248\u003c\/p\u003e \u003cp\u003e13.3.2 Surface Plasmon Resonance, 256\u003c\/p\u003e \u003cp\u003e13.4 Interrogating the Bio–Nano Interface, 256\u003c\/p\u003e \u003cp\u003e13.4.1 Atomic Force Microscopy, 256\u003c\/p\u003e \u003cp\u003e13.5 Outlook, 267\u003c\/p\u003e \u003cp\u003eAcknowledgment, 267\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 267\u003c\/p\u003e \u003cp\u003eReferences, 268\u003c\/p\u003e \u003cp\u003e\u003cb\u003e14 Scanning Electrochemical Microscopy for Biological Fuel Cell Characterization 273\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eRamaraja P. Ramasamy\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e14.1 Introduction, 273\u003c\/p\u003e \u003cp\u003e14.2 Theory and Operation, 274\u003c\/p\u003e \u003cp\u003e14.3 Ultramicroelectrodes, 275\u003c\/p\u003e \u003cp\u003e14.3.1 Approach Curve Method of Analysis, 276\u003c\/p\u003e \u003cp\u003e14.4 Modes of SECM Operation, 278\u003c\/p\u003e \u003cp\u003e14.4.1 Negative Feedback Mode, 278\u003c\/p\u003e \u003cp\u003e14.4.2 Positive Feedback Mode, 279\u003c\/p\u003e \u003cp\u003e14.4.3 Generation–Collection Mode, 279\u003c\/p\u003e \u003cp\u003e14.4.4 Induced Transfer Mode, 280\u003c\/p\u003e \u003cp\u003e14.5 SECM for BFC Anodes, 281\u003c\/p\u003e \u003cp\u003e14.5.1 Enzyme-Mediated Feedback Imaging, 281\u003c\/p\u003e \u003cp\u003e14.5.2 Generation–Collection Mode Imaging, 284\u003c\/p\u003e \u003cp\u003e14.6 SECM for BFC Cathodes, 285\u003c\/p\u003e \u003cp\u003e14.6.1 Tip Generation–Substrate Collection Mode, 286\u003c\/p\u003e \u003cp\u003e14.6.2 Redox Competition Mode, 289\u003c\/p\u003e \u003cp\u003e14.7 Catalyst Screening Using SECM, 290\u003c\/p\u003e \u003cp\u003e14.8 SECM for Membranes, 291\u003c\/p\u003e \u003cp\u003e14.9 Probing Single Enzyme Molecules Using SECM, 293\u003c\/p\u003e \u003cp\u003e14.10 Combining SECM with Other Techniques, 293\u003c\/p\u003e \u003cp\u003e14.10.1 Atomic Force Microscopy, 294\u003c\/p\u003e \u003cp\u003e14.10.2 Confocal Laser Scanning Microscopy, 295\u003c\/p\u003e \u003cp\u003e14.11 Outlook, 297\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 297\u003c\/p\u003e \u003cp\u003eReferences, 298\u003c\/p\u003e \u003cp\u003e\u003cb\u003e15 In Situ X-Ray Spectroscopy of Enzymatic Catalysis: Laccase-Catalyzed Oxygen Reduction 304\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eSanjeev Mukerjee, Joseph Ziegelbauer, Thomas M. Arruda, Kateryna Artyushkova, and Plamen Atanassov\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e15.1 Introduction, 304\u003c\/p\u003e \u003cp\u003e15.2 Defining the Enzyme\/Electrode Interface, 305\u003c\/p\u003e \u003cp\u003e15.3 Direct Electron Transfer Versus Mediated Electron Transfer, 306\u003c\/p\u003e \u003cp\u003e15.3.1 Mediated Electron Transfer, 307\u003c\/p\u003e \u003cp\u003e15.4 The Blue Copper Oxidases, 308\u003c\/p\u003e \u003cp\u003e15.4.1 Laccase, 309\u003c\/p\u003e \u003cp\u003e15.5 In Situ XAS, 310\u003c\/p\u003e \u003cp\u003e15.5.1 Os L3-Edge, 314\u003c\/p\u003e \u003cp\u003e15.5.2 uMET, 317\u003c\/p\u003e \u003cp\u003e15.5.3 Mediated Electron Transfer, 319\u003c\/p\u003e \u003cp\u003e15.5.4 FEFF8.0 Analysis, 323\u003c\/p\u003e \u003cp\u003e15.6 Proposed ORR Mechanism, 327\u003c\/p\u003e \u003cp\u003e15.7 Outlook, 331\u003c\/p\u003e \u003cp\u003eAcknowledgments, 331\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 331\u003c\/p\u003e \u003cp\u003eReferences, 332\u003c\/p\u003e \u003cp\u003e\u003cb\u003e16 Enzymatic Fuel Cell Design, Operation, and Application 337\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eVojtech Svoboda and Plamen Atanassov\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e16.1 Introduction, 337\u003c\/p\u003e \u003cp\u003e16.2 Biobatteries and EFCs, 338\u003c\/p\u003e \u003cp\u003e16.3 Components, 339\u003c\/p\u003e \u003cp\u003e16.3.1 Anodes, 339\u003c\/p\u003e \u003cp\u003e16.3.2 Cathodes, 340\u003c\/p\u003e \u003cp\u003e16.3.3 Separator and Membrane, 341\u003c\/p\u003e \u003cp\u003e16.3.4 Reference Electrode, 342\u003c\/p\u003e \u003cp\u003e16.3.5 Fuel and Electrolyte, 342\u003c\/p\u003e \u003cp\u003e16.4 Single-Cell Design, 345\u003c\/p\u003e \u003cp\u003e16.4.1 Design of Single-Cell EFC Compartment, 345\u003c\/p\u003e \u003cp\u003e16.5 Microfluidic EFC Design, 348\u003c\/p\u003e \u003cp\u003e16.6 Stacked Cell Design, 348\u003c\/p\u003e \u003cp\u003e16.6.1 Series-Connected EFC Stack, 348\u003c\/p\u003e \u003cp\u003e16.6.2 Parallel-Connected EFC Stack, 349\u003c\/p\u003e \u003cp\u003e16.7 Bipolar Electrodes, 350\u003c\/p\u003e \u003cp\u003e16.8 Air\/Oxygen Supply, 351\u003c\/p\u003e \u003cp\u003e16.9 Fuel Supply, 351\u003c\/p\u003e \u003cp\u003e16.9.1 Fuel Flow-Through, 352\u003c\/p\u003e \u003cp\u003e16.9.2 Fuel Flow-Through System, 354\u003c\/p\u003e \u003cp\u003e16.9.3 Fuel Flow-Through Operation and Fuel Waste Management, 355\u003c\/p\u003e \u003cp\u003e16.10 Storage and Shelf Life, 356\u003c\/p\u003e \u003cp\u003e16.11 EFC Operation, Control, and Integration with Other Power Sources, 356\u003c\/p\u003e \u003cp\u003e16.11.1 Activation, 356\u003c\/p\u003e \u003cp\u003e16.12 EFC Control, 357\u003c\/p\u003e \u003cp\u003e16.13 Power Conditioning, 357\u003c\/p\u003e \u003cp\u003e16.14 Outlook, 358\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 359\u003c\/p\u003e \u003cp\u003eReferences, 359\u003c\/p\u003e \u003cp\u003e\u003cb\u003e17 Miniature Enzymatic Fuel Cells 361\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eTakeo Miyake and Matsuhiko Nishizawa\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e17.1 Introduction, 361\u003c\/p\u003e \u003cp\u003e17.2 Insertion MEFC, 362\u003c\/p\u003e \u003cp\u003e17.2.1 Insertion MEFC with Needle Anode and Gas Diffusion Cathode, 363\u003c\/p\u003e \u003cp\u003e17.2.2 Windable, Replaceable Enzyme Electrode Films, 364\u003c\/p\u003e \u003cp\u003e17.3 Microfluidic MEFC, 366\u003c\/p\u003e \u003cp\u003e17.3.1 Effects of Structural Design on Cell Performances, 366\u003c\/p\u003e \u003cp\u003e17.3.2 Automatic Air Valve System, 367\u003c\/p\u003e \u003cp\u003e17.3.3 SPG System, 369\u003c\/p\u003e \u003cp\u003e17.4 Flexible Sheet MEFC, 370\u003c\/p\u003e \u003cp\u003e17.5 Outlook, 371\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 372\u003c\/p\u003e \u003cp\u003eReferences, 372\u003c\/p\u003e \u003cp\u003e\u003cb\u003e18 Switchable Electrodes and Biological Fuel Cells 374\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eEvgeny Katz, Vera Bocharova, and Jan Halámek\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e18.1 Introduction, 374\u003c\/p\u003e \u003cp\u003e18.2 Switchable Electrodes for Bioelectronic Applications, 375\u003c\/p\u003e \u003cp\u003e18.3 Light-Switchable Modified Electrodes Based on Photoisomerizable Materials, 376\u003c\/p\u003e \u003cp\u003e18.4 Magnetoswitchable Electrochemical Reactions Controlled by Magnetic Species Associated with Electrode Interfaces, 378\u003c\/p\u003e \u003cp\u003e18.5 Modified Electrodes Switchable by Applied Potentials Resulting in Electrochemical Transformations at Functional Interfaces, 381\u003c\/p\u003e \u003cp\u003e18.6 Chemically\/Biochemically Switchable Electrodes, 383\u003c\/p\u003e \u003cp\u003e18.7 Coupling of Switchable Electrodes with Biomolecular Computing Systems, 389\u003c\/p\u003e \u003cp\u003e18.8 BFCs with Switchable\/Tunable Power Output, 396\u003c\/p\u003e \u003cp\u003e18.8.1 Switchable\/Tunable BFCs Controlled by Electrical Signals, 397\u003c\/p\u003e \u003cp\u003e18.8.2 Switchable\/Tunable BFCs Controlled by Magnetic Signals, 399\u003c\/p\u003e \u003cp\u003e18.8.3 BFCs Controlled by Logically Processed Biochemical Signals, 402\u003c\/p\u003e \u003cp\u003e18.9 Outlook, 412\u003c\/p\u003e \u003cp\u003eAcknowledgments, 413\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 413\u003c\/p\u003e \u003cp\u003eReferences, 414\u003c\/p\u003e \u003cp\u003e\u003cb\u003e19 Biological Fuel Cells for Biomedical Applications 422\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eMagnus Falk, Sergey Shleev, Claudia W. Narváez Villarrubia, Sofia Babanova, and Plamen Atanassov\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e19.1 Introduction, 422\u003c\/p\u003e \u003cp\u003e19.2 Definition and Classification of BFCs, 424\u003c\/p\u003e \u003cp\u003e19.2.1 Cell- and Organelle-Based Fuel Cells, 425\u003c\/p\u003e \u003cp\u003e19.2.2 Enzymatic Fuel Cells, 426\u003c\/p\u003e \u003cp\u003e19.3 Design Aspects of EFCs, 427\u003c\/p\u003e \u003cp\u003e19.3.1 Electron Transfer, 427\u003c\/p\u003e \u003cp\u003e19.3.2 Enzymes, 428\u003c\/p\u003e \u003cp\u003e19.3.3 Electrodes and Electrode Materials, 430\u003c\/p\u003e \u003cp\u003e19.3.4 Biodevice Design, 431\u003c\/p\u003e \u003cp\u003e19.4 In Vitro and In Vivo BFC Studies, 433\u003c\/p\u003e \u003cp\u003e19.4.1 In Vitro BFCs, 433\u003c\/p\u003e \u003cp\u003e19.4.2 In Vivo Operating BFCs, 435\u003c\/p\u003e \u003cp\u003e19.5 Outlook, 440\u003c\/p\u003e \u003cp\u003eList of Abbreviations, 442\u003c\/p\u003e \u003cp\u003eReferences, 443\u003c\/p\u003e \u003cp\u003e\u003cb\u003e20 Concluding Remarks and Outlook 451\u003c\/b\u003e\u003cbr\u003e \u003ci\u003eGlenn R. Johnson, Heather R. Luckarift, and Plamen Atanassov\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e20.1 Introduction, 451\u003c\/p\u003e \u003cp\u003e20.2 Primary System Engineering: Design Determinants, 453\u003c\/p\u003e \u003cp\u003e20.3 Fundamental Advances in Bioelectrocatalysis, 454\u003c\/p\u003e \u003cp\u003e20.4 Design Opportunities from EFC Operation, 454\u003c\/p\u003e \u003cp\u003e20.5 Fundamental Drivers for EFC Miniaturization, 455\u003c\/p\u003e \u003cp\u003e20.6 Commercialization of EFCs: Strategies and Opportunities, 455\u003c\/p\u003e \u003cp\u003e\u003ci\u003eAcknowledgment, 457\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003ci\u003eList of Abbreviations, 457\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003ci\u003eReferences, 457\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003ci\u003eIndex 459\u003c\/i\u003e\u003c\/p\u003e","brand":"John Wiley \u0026 Sons Inc","offers":[{"title":"Default Title","offer_id":49528827281751,"sku":"9781118369234","price":106.35,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781118369234.jpg?v=1731873174","url":"https:\/\/bookcurl.com\/products\/enzymatic-fuel-cells-from-fundamentals-to-applications-9781118369234","provider":"Book Curl","version":"1.0","type":"link"}