Kularatna Energy Storage Devices for Electronic Systems

Rechargeable Batteries and Supercapacitors
1. Auflage 2014
ISBN: 978-0-12-408119-2
Verlag: Elsevier Science & Techn.
Format: EPUB
Kopierschutz: 6 - ePub Watermark

E-Book, Englisch, 320 Seiten

Energy storage devices are a crucial area of research and development across many engineering disciplines and industries. While batteries provide the significant advantage of high energy density, their limited life cycles, disposal challenges and charge and discharge management constraints undercut their effectiveness in certain applications. Compared to electrochemical cells, supercapacitors are charge-storage devices with much longer life cycles, yet they have traditionally been hobbled by limited DC voltage capabilities and energy density. However, recent advances are improving these issues. This book provides the opportunity to expand your knowledge of innovative supercapacitor applications, comparing them to other commonly used energy storage devices. It will strengthen your understanding of energy storage from a practical, applications-based point-of-view, without requiring detailed examination of underlying electrochemical equations. No matter what your field, you will find inspiration and guidance in the cutting-edge advances in energy storage devices in this book. - Provides explanations of the latest energy storage devices in a practical applications-based context - Includes examples of circuit designs that optimize the use of supercapacitors, and pathways to improve existing designs by effectively managing energy storage devices crucial to both low and high power applications. - Covers batteries, BMS (battery management systems) and cutting-edge advances in supercapacitors, providing a unique compare and contrast examination demonstrating applications where each technology can offer unique benefits

Nihal Kularatna is an Associate Professor in the School of Engineering at the University of Waikato, New Zealand. He won the New Zealand Innovator of the Year Award (2013). His electronic engineering career spans 45 years and he is currently active in research in supercapacitor applications, power converter topologies, and power conditioning. He has contributed to over 160 papers and authored nine books. Multiple patents were granted for his supercapacitor assisted (SCA) circuit topologies. Before migrating to New Zealand in 2002, he was the CEO of the Arthur C Clarke Institute in Sri Lanka.

Autoren/Hrsg.

Kularatna, Nihal

Inhaltsverzeichnis

1;Front Cover;1
2;The Myocardium;4
3;Copyright Page;5
4;Contents;8
5;Contributors;14
6;Preface to the Second Edition;16
7;Preface to the First Edition;18
8;Chapter 1. Immunolocalization and Structural Configuration of Membrane and Cytoskeletal Proteins Involved in Excitation–Contraction Coupling of Cardiac Muscle;20
8.1;I. Introduction;20
8.2;II. Ca Receptors, Channels, Releasers, and Storage;21
8.3;III. Subcellular Localization of Cardiac Membrane Exchangers;30
8.4;IV. Cytoskeleton;44
8.5;References;51
9;Chapter 2. Myocardial Cellular Development and Morphogenesis;56
9.1;I. Introduction;56
9.2;II. Early Cardiac Myogenesis;57
9.3;III. Diversification and Specification of Myocytes;65
9.4;IV. Proliferation of Cardiac Myocytes;71
9.5;V. Hypertrophic Response to Increased Demand;80
9.6;Acronyms and Abbreviations;92
9.7;References;94
10;Chapter 3. Ion Channels in Cardiac Muscle;104
10.1;I. Introduction;104
10.2;II. Cardiac Ion Channels;105
10.3;III. Cardiac Action Potential: Formation and Propagation;142
10.4;IV. Future Challenges;156
10.5;References;156
11;Chapter 4. Myocardial Ion Transporters;166
11.1;I. Introduction;166
11.2;II. The Players;167
11.3;III. P-Type Ion Pumps;167
11.4;IV. The ATP-Dependent Na+ Pump;169
11.5;V. The Plasma Membrane ATP-Dependent Ca2+ Pump;178
11.6;VI. The Sarcoplasmic Reticular ATP-Dependent Ca2+ Pump;183
11.7;VII. Na+–Ca2+ Exchange;188
11.8;VIII. Other Transporters: Na+–H+ Exchange;196
11.9;IX. Perspectives;198
11.10;References;198
12;Chapter 5. Excitation–Contraction Coupling and Calcium Compartmentation;204
12.1;I. Introduction;204
12.2;II. Extracellular Calcium;204
12.3;III. Subcellular Calcium Compartmentation;206
12.4;IV. Calcium Movement in Subsarcolemmal Diadic Cleft;220
12.5;V. Calcium in the Cytoplasm;231
12.6;VI. Drugs and Calcium;235
12.7;VII. Calcium Movement in the Cell;243
12.8;VIII. Calcium in the Metabolically Compromised Cell;245
12.9;IX. The Future;249
12.10;References;250
13;Chapter 6. Mechanics and Force Production;258
13.1;I. Introduction;258
13.2;II. Cellular Structure—Mechanical Aspects;260
13.3;III. Myofilaments as Force Generators—Molecular Motors;269
13.4;IV. Myofilaments as Regulators of Force Generation;283
13.5;V. Cellular Function—Systolic and Diastolic Properties of Cells;297
13.6;References;331
14;Chapter 7. Metabolism in Normal and Ischemic Myocardium;348
14.1;I. Introduction;348
14.2;II. Normal Myocardial Metabolism;349
14.3;III. Metabolic Regulation of Cellular Processes by Glycolytic and Oxidative Metabolism;354
14.4;IV. Myocardial Ischemia;370
14.5;V. Reperfusion of Ischemic Tissue: Metabolic and Functional Issues;383
14.6;References;398
15;Index;418

Leseproben

1 Immunolocalization and Structural Configuration of Membrane and Cytoskeletal Proteins Involved in Excitation-Contraction Coupling of Cardiac Muscle
Joy S. Frank; Alan Garfinkel I INTRODUCTION
The focus of this chapter is on the structures involved in excitation–contraction (E-C) coupling. This is not intended to be a comprehensive review but does cover areas that have been of particular interest to the Cardiovascular Research Laboratory at UCLA School of Medicine and that are particularly related to the other chapters in this book. The structure of key functional units in E-C coupling is covered, especially the transverse (T) tubules, junctional and corbular sarcoplasmic reticulum (SR), and the diadic space formed by the close apposition of the sarcolemma (SL) and the junctional sarcoplasmic reticulum (jSR). In addition, the subcellular localization of proteins involved in the regulation of intracellular Ca2 + are discussed. This includes the distribution of the Na+ - Ca2 + exchanger, Na+K+ATPase, the Ca2 + release channel/ryanodine receptor (CRC/RR), and the Ca2 + channel (DHP receptor). The organization of proteins within regions of the SL or SR results in domains of functional significance. Thus a discussion on the role of cytoskeletal proteins and their relationship to Ca regulatory proteins completes the chapter. II Ca RECEPTORS, CHANNELS, RELEASERS, AND STORAGE
A DIADIC CLEFT
The region where the SL and the SR appose each other contains the most important functional units for the coupling of excitation to contraction. The close apposition of the lateral cistern of the jSR to the SL defines a space (~ 15 nm) containing channels, receptors, and exchangers whose function revolves around the regulation of Ca flux into and out of the myocyte. For all its importance, this space and the membranes that restrict it have lacked an all-encompassing name. Lederer et al. (1990) coined the term fuzzy space for this region. Langer and Peskoff (1996) have designated this space the diadic cleft and have produced a working model of its structural and functional characteristics (see Chapter 5). 1 Ca Release Channel/Ryanodine Receptor The membrane of the jSR facing the SL has regularly arranged projections or “foot” processes (Franzini-Armstrong, 1980) that extend ~ 12 nm into the diadic cleft to contact the membrane of the T tubule forming an interior coupling or to contact the surface SL to form a peripheral coupling. The structure and function of these junctional spanning proteins or “feet” have been studied in great detail (Franzini-Armstrong, 1980; Kelly and Kuda, 1979; Lai et al, 1988; Anderson et al, 1989). It is well accepted that the feet that are periodically arrayed in the diadic cleft contain the ryanodine receptor (RR), a high-conductance calcium channel that provides for the release of calcium ions from the SR during contraction (Ogawa, 1994; Anderson et al, 1989). Figure 1 contains two useful images of the diadic cleft. Figure 1A is a thin-section electron micrograph from rabbit papillary muscle. It is from this conventional type of preparation that the feet were first visible, due partly to the fact that they are equally spaced along the jSR. Figure 1B presents a more three-dimensional (3-D) perspective of the structure of the diadic cleft. The tissue is prepared here with freeze-fracture/deep-etching on cells that are not chemically preserved but ultrarapidly frozen. An “end-on view” of the feet/calcium release channel (CRC) can easily be seen to span the cleft bridging the jSR and the T tubular membrane. Immunolabeling studies with antibodies against the RR have localized the CRC/RR in adult cardiac muscle predominantly at the level of the T tubules, in clearly defined banding pattern at the Z lines [Figs. 2A and B]. Figure 1 Ultrastructure of diadic cleft—rabbit papillary muscle. (A) An electron micrograph from thin-sectioned, conventionally prepared tissue. The specialized junction between the transverse tubule (TT) and the junctional side of the sarcoplasmic reticulum (SR) is clearly seen. Spanning the diadic cleft are regularly arrayed “feet” (arrows), which contain the Ca2 + release channels/ryanodine receptors (CRC/RRs). MIT, mitochondria. Original magnification x126,360. (B) An electron micrograph from tissue that was ultrarapidly frozen, fractured, and deep etched. The same structures seen in A are now visible in a 3-D perspective. The arrowhead points to the fractured lumen of the TT. The arrows clearly show the “feet” structures spanning the gap between the TT membrane and the junctional SR membrane, and contain the CRC/ RRs. MIT, mitochondria. Original magnification x126,360. (Reprinted with permission from Frank, 1990.) Figure 2A A Immunolocalization of the ryanodine receptor. Isolated rat myocyte labeled with antibodies against the CRC/RR. Immunofluorescence is clearly visible in this confocal micrograph as regularly spaced transverse bands. This localizes the CRC/RR at the level of the Z-disc and in association with the T tubular portion of the SL. Original magnification x 1500. (See Fig. 2B.) Figure 2B Three-dimensional reconstruction of CRC/RR localization within a rat myocyte. Red “hot spots” seen here along the regularly arrayed cross bands represent areas of highest fluorescent intensity and presumably the highest number of CRC/RR sites. A series of confocal “slices” were taken at 0.5 µm intervals through an isolated rat myocyte exposed to antibodies against the CRC/RR as seen in 2A. These slices were used to construct this 3-D reconstruction. Volume rendering and gradient-based ray casting techniques were used to visualize the high-intensity regions (see Bacallao and Garfinkel, 1994, and Fig. 9, for more details). The large tetrameric CRC/RR ion channel complex has been isolated from skeletal muscle. With the use of the isolated channels, Radermacher et al. (1994) were able to obtain frozen hydrated samples that were used for cryo-electron microscopy to produce excellent preservation of the macromolecular ultrastructure of the channels. With 3-D reconstruction techniques, the most detailed view to date of the CRC structure was produced. The “foot” portion of the CRC is a large assembly (29 × 29 × 12 nm) linked to a smaller transmembrane component. The resolution afforded by the 3-D reconstruction is such that a cylindrical, low-density region extending down the center of the foot assembly could be discerned and most likely corresponds to the Ca2 + conducting pathway (Fig. 3). Figure 3 The 3-D architecture of the CRC/RR depicted from surface representations given here as stereo pairs. (a) This view shows the surface that would face the cytoplasm and the apposing T tubule in a triad junction. (b) This view shows the face that would interact with the jSR. (c) This is a side view. The protein that forms the cytoplasmic assembly appears to be arranged as domains that are loosely packed together and have been given numerical labels depicted on the right-sided pair. The other labeling is cc, central cavity, and p, plug feature that appears to be a globular mass in the center of the channel that the authors refer to as “channel plug.” The plug is surrounded by four small cavities that lead to the exterior of the transmembrane assembly, labeled as pc for peripheral cavity. Bar = 10 nm. (Reproduced from The Journal of Cell Biology, 1994, vol. 127, p. 419, by copyright permission of The Rockefeller University Press.) In skeletal muscle, at least, there is good structural evidence for a direct interaction between the CRC/RR and the Ca2 + channels (DHP receptors) located within the T tubular membrane. This is an important point because the mechanism of excitation—contraction (E-C) coupling in skeletal muscle is believed to occur by sarcolemmal depolarization acting on the DHP receptors, which in turn act as voltage sensors (Leung et al., 1988; Rios and Brum, 1987) that undergo a confirmation change. It is this direct molecular interaction that is believed to induce the opening of the CRC/RR and thus the release of calcium from the jSR. Block et al. (1988) identified large intramembrane particles (IMPs) in the P face (membrane face adjacent to the cytoplasm) of the T tubular membrane in skeletal muscle. These are the only intramembraneous particles seen in the T tubular membrane, and they have the characteristics of the DHP receptors. In addition, skeletal muscle T tubular membranes are the richest source of DHP receptors. This adds additional support to the idea that these particles represent the DHP receptors. Interestingly, the particles are arrayed in clusters of four particles forming a tetrad. The axis of fourfold symmetry is rotated and, as a result, each tetrad of IMPs in the tubular membrane is opposite alternating foot structures of the CRC/RR. This structural arrangement between the CRC/ RR in the jSR and the DHP receptors in the T tubular membrane provides direct support for the...