Frontiers of Cellular Bioenergetics: Molecular Biology, Biochemistry, and Physiopathology,9780306458514

Frontiers of Cellular Bioenergetics: Molecular Biology, Biochemistry, and Physiopathology

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Edition: 1st
ISBN13: 9780306458514
ISBN10: 0306458519
Format: Hardcover
Pub. Date: 1999-05-01
Publisher(s): PLENUM PUBLISHING
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Summary

Univ. of Bari, Italy. Discusses the physiopathological aspects of mitochondria as well as with the role of the mitochondrial permiability transition pore in apoptosis. For students, researchers, and clinicians. Extensive references and halftone illustrations are included. Expanded-outline format.

Table of Contents

The Mitochondrial and Bacterial Respiratory Chains: From MacMunn and Keilin to Current Concepts
1(22)
Peter Nicholls
Cellular Respiration before the Chain
1(1)
The Coming of the Respiratory Chain
2(1)
The Discovery of the Cytochrome System
3(4)
High Noon for the Respiratory Chain
7(1)
Membrane Location of the Respiratory Chain
8(3)
Breaking the Respiratory Chain into Complexes
11(2)
Reconstituting the Respiratory Chain from Its Parts
13(1)
Transforming the Respiratory Chain into a Transmembranous Electron and Proton Transfer System
14(4)
Opening the Black Boxes that Have Replaced the Chain
18(2)
References
20(3)
The Mitochondrial Enzymes of Oxidative Phosphorylation
23(26)
Youssef Hatefi
Introduction
23(2)
Complex I (NADH--Quinone Oxidoreductase)
25(4)
Composition
25(1)
Structure
26(1)
Enzymatic Properties
27(2)
Complex II (Succinate--Quinone Oxidoreductase)
29(5)
Composition and Structure of Complex II
29(2)
Enzymatic Properties
31(2)
Cytochrome b of Complex II
33(1)
Complex III (Quinol--Cytochrome c Oxidoreductase)
34(4)
General Features
34(1)
Mechanisms of Electron Transfer and Proton Translocation
35(3)
Complex V (ATP Synthase Complex)
38(5)
Composition and Structure
39(2)
Enzymatic Properties
41(1)
Conformational Energy Transfer in the ATP Synthase
42(1)
References
43(6)
Proton Pumps of Respiratory Chain Enzymes
49(40)
Sergio Papa
Nazzareno Capitanio
Gaetano Villani
Introduction
49(5)
The Output Efficiency of Redox Proton Pumps
54(7)
Redox Bohr Effects and Cooperative Coupling in Cytochrome c Oxidase
61(7)
Role of Noncatalytic Subunits in Heme--Copper Oxidases
68(3)
A Cooperative Proton Pump in Heme--Copper Oxidases
71(8)
Possible Mechanisms of the Proton Pump in Complexes I and III
79(3)
References
82(7)
Uncoupling of Respiration and Phosphorylation
89(30)
Vladimir P. Skulachev
Definitions
89(1)
Artificial Uncouplers
90(4)
Natural Uncouplers
94(5)
Fatty Acids
94(4)
Other Natural Uncouplers and Uncoupling Systems
98(1)
Physiological Aspects of Uncoupling
99(6)
Endogenous Uncoupling
99(1)
Multiple Functions of Cellular Respiration
100(1)
Thermoregulatory Uncoupling
100(1)
Noncoupled Respiration: Anabolic and Catabolic Functions
101(1)
Possible Role of Uncoupling in the Anti-ROS Defense System
102(3)
Stimulation of ATP Synthesis by Partial Uncoupling
105(1)
Pathological Aspects of Uncoupling
105(2)
Addendum
107(3)
References
110(9)
Crystallization, Structure, and Possible Mechanism of Action of Cytochrome c Oxidase from the Soil Bacterium Paracoccus denitrificans
119(12)
Hartmut Michel
So Iwata
Christian Ostermeier
Introduction
119(2)
Crystallization
121(1)
The Structure of the Paracoccus Cytochrome c Oxidase
121(5)
The Structure of the Protein Subunits
123(1)
The Structure of the Metal Centers
124(2)
Possible Mechanisms
126(3)
References
129(2)
The Structure of Crystalline Bovine Heart Cytochrome c Oxidase
131(26)
Shinya Yoshikawa
Kyoko Shinzawa-Itoh
Tomitake Tsukihara
Introduction
131(1)
An Overview of the Crystal Structure of Beef Heart Cytochrome c Oxidase
132(2)
Structure of the Redox Active Metal Sites and the Electron Transfer between Them
134(8)
CuA Site
134(3)
Hydroxylfarnesylethyl Groups
137(1)
Magnesium Site
138(1)
Heme a and the O2 Reduction Site
138(4)
Electron Transfers between the Three Redox Centers
142(1)
Mechanism of the O2 Reduction and the Role of CuB
142(4)
Mechanism of Proton Pumping
146(3)
Phospholipids and Cholate
149(1)
Roles of Subunits Other Than Subunits I and II
150(3)
Subunit III
150(1)
Nuclear-Encoded Subunits
150(1)
Subunits for Dimer Formation and ADP Binding
151(1)
Cytochrome c Binding Site
152(1)
References
153(4)
Electron and Proton Transfer in Heme--Copper Oxidases
157(22)
Yuejun Zhen
Denise A. Mills
Curtis W. Hoganson
Rebecca Lucas
Wenjun Shi
Gerald T. Babcock
Shelagh Ferguson-Miller
Introduction
157(1)
Electron Pathways and Control of Electron Transfer
158(7)
General Characteristics of Subunit II Mutants
159(2)
Surface Charge Changes Close to CuA: Effects on Cytochrome c Interaction
161(1)
Decoupling of the Binuclear CuA Site: Effects on Electron Transfer and Proton Pumping
162(2)
Disruption of a Putative ``Through-Bond'' Pathway
164(1)
Conclusions
165(1)
Proton Pathways and Control of Pumping Efficiency
165(10)
Mutants at Aspartate 132 in Rhodobacter sphaeroides Cytochrome c Oxidase
166(7)
Regulation of the Efficiency of Bovine Oxidase by ATP
173(1)
Conclusion
174(1)
Summary
175(1)
References
175(4)
Mechanism of Proton-Motive Activity of Heme--Copper Oxidases
179(14)
Peter R. Rich
Introduction
179(1)
Principles of Coupling
180(1)
The Importance of Local Electroneutrality within the Reaction Core
181(2)
Internal Charge Balancing and Proton-Motive Mechanism
183(1)
Gating of the Proton Transfer Route
184(1)
Charge-Linked Protonation Sites and Structural Features
184(2)
Chemical Models for Proton Translocation
186(4)
The Histidine Cycle
186(1)
The Glutamate Trap
187(1)
Experimental Progress
188(2)
References
190(3)
Oxygen Reduction and Proton Translocation by the Heme--Copper Oxidases
193(26)
Marten Wikstrom
Joel E. Morgan
Gerhard Hummer
William H. Woodruff
Michael I. Verkhovsky
Introduction
193(1)
Structure
194(4)
Subunit III
194(1)
Subunit II
194(1)
Subunit I and the Binuclear Site
195(3)
The Catalytic Cycle
198(5)
Kinetics and Reaction Intermediates
198(2)
The Structures of F and P
200(2)
Proton Consumption
202(1)
Proton Translocation (Pumping)
203(1)
Mechanistic Linkage of Proton Translocation to Catalysis
203(9)
The Reactions that Are Linked to Proton Translocation
204(1)
Transfer versus Translocation of Protons
204(1)
Proton Channels and Water Chains
205(2)
Proton Translocation and the Histidine Cycle
207(1)
Formation of the PR State
208(1)
Discharge of the PR State
209(1)
The Shuttling of Imidazole
210(1)
Conversion of the Ferryl State to the Oxidized Enzyme
211(1)
Epilogue
212(1)
References
212(7)
Transient Spectroscopy of the Reaction between Cytochrome c Oxidase and Nitric Oxide: A New Hypothesis on the Mechanism of Inhibition and Oxygen Competition
219(14)
Alessandro Giuffre
Paolo Sarti
Emilio D'Itri
Gerhard Buse
Tewfik Soulimane
Maurizio Brunori
Introduction
219(2)
Materials and Experimental Designs
221(2)
General Information
221(1)
The Photodiode Array Experiments
222(1)
The Sequential Mixing Experiments
223(1)
Results and Discussion
223(8)
The Oxygen-Dependent Reversibility of Cytochrome Oxidase Inhibition by NO
223(2)
The Onset of Inhibition
225(1)
The Spectral Intermediates Populated during Turnover and Nitrosylation
226(2)
Determining the NO Off Rate
228(2)
The Mechanism of Interaction between NO and Cytochrome Oxidase
230(1)
Concluding Remarks
231(1)
References
232(1)
Energy Transduction in Mitochondrial Respiration by the Proton-Motive Q-Cycle Mechanism of the Cytochrome bc1 Complex
233(30)
Bernard L. Trumpower
The Crystal Structure of Mitochondrial Cytochrome bc1 Complex
263(28)
Chang-An Yu Li Zhang
Anatoly M. Kachurin
Sudha K. Shenoy
Kai-Ping Deng
Linda Yu
Di Xia
Hoeon Kim
Johann Deisenhofer
Introduction
263(2)
Preparation and Crystallization of the Cytochrome bc1 Complex
265(3)
Preparation and Properties
265(1)
Crystallization and Data Collection
266(2)
Cocrystallization of the Cytochrome bc1 Complex with Inhibitors
268(1)
Cocrystallization of the Cytochrome bc1 Complex with Cytochrome c
268(1)
Structure Analysis of the Cytochrome bc1 Complex by X-Ray Diffraction
268(11)
Structure Overview
268(2)
Localization of Redox Centers
270(2)
Localization of Inhibitor Binding Sites
272(2)
Intermembrane Space Region: Cytochrome c1 and ISP
274(1)
Membrane-Spanning Region: Cytochrome b
275(2)
Matrix Region and Core Proteins
277(2)
Protein-Processing Peptidase Activity
279(2)
MPP Activity of the Cytochrome bc1 Complex
279(2)
Cloning, Overexpressing, and in Vitro Reconstitution of MPP from Core Proteins
281(1)
Structural Basis of the Electron Transfer Reaction
281(5)
Does the Cytochrome bc1 Complex Function as a Dimer or a Monomer
281(1)
Ubiquinone Binding Sites
282(1)
Electron Transfer Rate and Distances between the Redox Centers
283(1)
Movement of Iron--Sulfur Protein
283(1)
Electron Transfer Events at the Q0 Site
284(1)
Proton Translocation: Pumping/Gating
285(1)
Assembly of Mitochondrial Cytochrome bc1 Complex
285(1)
References
286(5)
Structural Aspects of the Cytochrome bc1 Complex
291(34)
Thomas A. Link
Introduction
291(1)
Subunits and Their Phylogenetic Relationship
292(5)
Subunits Containing Redox Centers
292(3)
Subunits without Redox Centers
295(2)
Other Constituents
297(1)
Structures of the Catalytic Subunits and the Redox Centers
297(10)
Cytochrome b
297(4)
Cytochrome c1
301(1)
``Rieske'' Iron--Sulfur Protein
302(5)
General Topology and Orientation of the Redox Centers
307(2)
Quinone Reaction and Inhibitor Binding Sites
309(8)
Quinone Reduction (QN) Site
311(1)
Hydroquinone Oxidation (QP) Site
312(5)
Summary and Perspective
317(1)
References
318(7)
Structure, Function, and Biogenesis of Respiratory Complex I
325(36)
Ulrich Schulte
Hanns Weiss
Introduction
325(1)
Structure of Complex I
326(7)
Genes and Subunits
326(2)
Prosthetic Groups
328(3)
Three-Dimensional Structure and Subunit Arrangement
331(2)
Function of Complex I
333(5)
Electron Transfer
333(3)
Proton Translocation
336(2)
Inhibitors
338(1)
Biogenesis of Complex I
338(10)
Assembly Intermediates
338(2)
Subunits Involved in a Biosynthetic Pathway
340(8)
Origin and Evolution of Complex I
348(2)
Perspectives
350(1)
References
351(10)
Structure of F1-ATPase and the Mechanism of ATP Synthesis--Hydrolysis
361(16)
Mario A. Bianchet
Peter L. Pedersen
L. Mario Amzel
Introduction
361(2)
Structure of F1-ATPase
363(8)
Overall Structure
364(3)
Nucleotide Binding Sites
367(4)
Mechanism of ATP Synthesis--Hydrolysis
371(4)
References
375(2)
Mechanism of ATP Synthesis by Mitochondrial ATP Synthase
377(22)
Abdul-Kader Souid
Harvey S. Penefsky
Introduction
377(2)
Thermodynamic Relationships in Oxidative Phosphorylation
379(4)
Rate Constants, Equilibrium Constants, and Free Energy Changes during ATP Synthesis
383(2)
Utilization of Intrinsic Binding Energy and the Binding Change Mechanism
385(2)
Kinetic Aspects of Unisite Catalysis
387(2)
Energy-Dependent Dissociation of Product ATP from High-Affinity Catalytic Sites
389(3)
References
392(7)
Mutational Analysis of ATP Synthase: An Approach to Catalysis and Energy Coupling
399(24)
Masamitsu Futai
Hiroshi Omote
Introduction
399(2)
Catalysis and Catalytic Sites in the F1 Sector
401(7)
ATP Synthesis and Hydrolysis by F0F1
401(1)
βLys-155 and βThr-156 Are Catalytic Residues
402(2)
βGlu-181, βArg-182, and βGlu-185 in the Conserved GER XXE Sequence Are Catalytic Residues
404(2)
Interaction(s) between the α and β Subunits
406(2)
The γSubunit in Catalysis and Energy Coupling
408(6)
Mutations in the γ Subunit Cause Defective Catalysis and Assembly
408(1)
Roles of the γ Subunit in Energy Coupling
409(1)
Interactions between the β and γ Subunits
410(2)
The Stalk Region of F0F1
412(2)
Summary
414(1)
References
415(8)
Analysis of the Nucleotide Binding Sites of ATP Synthase and Consequences for the Catalytic Mechanism
423(36)
J. A. Berden
A. F. Hartog
Introduction
423(2)
Relevant Elements in the Characterization of Nucleotide Binding Sites
425(3)
The Different Aspects of Nucleotide Binding
425(1)
Different Types of F1 Preparations
426(2)
Properties of the Nucleotide Binding Sites of MF1
428(14)
Characterization of Nucleotide Binding Sites on Basis of Affinity and Exchangeability
428(6)
Characterization of Binding Sites on Basis of Localization
434(3)
Characterization of Binding Sites on Basis of Catalytic Involvement
437(5)
Nucleotide Binding Sites and Catalysis
442(5)
A Model of the Nucleotide Binding Sites of MF1 and Consequences for the Catalytic Mechanism
442(3)
Possible Role of the Nucleotide Binding Sites in Catalysis of ATP Synthesis
445(2)
Interpretation of Some Data Reported to Be Indicative for a Three-Site Mechanism of Catalysis
447(3)
Conclusions: A Proposal for the Overall Mechanism of the ATP Synthase
450(1)
References
451(8)
Coupling Structures and Mechanisms in the Stalk of the Bovine Mitochondrial F0F1-ATP Synthase
459(30)
Sergio Papa
Ting Xu
Antonio Gaballo
Franco Zanotti
Introduction
459(3)
The Subunits Constituting the Stalk and Their Stoichiometry
462(7)
The Proton Gate in the Stalk
469(3)
Near-Neighbor Relationships of Stalk Subunits
472(3)
The Stalk, Energy-Coupling, and Rotatory Motor in the ATP Synthase
475(7)
References
482(7)
The Mitochondrial Carrier Protein Family
489(32)
Ferdinando Palmieri
Ben van Ommen
Introduction
489(1)
Primary Structure and Extension of the Family
490(6)
Secondary Structure and Transmembrane Topology
496(3)
Expression
499(1)
The Yeast Genome: 35 Carrierlike Sequences
499(1)
Genomic Structure and Evolution
500(2)
Structure and Function Studies: The Use of Mutant Proteins
502(6)
Role of Cysteines
504(1)
Role of Charged Residues
505(2)
Role of Tryptophan Residues
507(1)
Mutations that Affect Carrier Regulation
507(1)
Biogenesis of Mitochondrial Metabolite Carriers
508(1)
The Carnitine Carrier: A Fatal Genetic Disorder
509(1)
Conclusions and Perspectives
510(1)
References
511(10)
Structure and Evolution of the Metazoan Mitochondrial Genome
521(32)
Cecilia Saccone
General Features of the Mitochondrial Genome in Various Organisms
522(4)
Genome Shape and Size
522(1)
Genome Organization
523(3)
The Evolution of the Mitochondrial DNA in Metazoa
526(9)
Completely Sequenced Genomes
526(1)
Variation between Phyla
526(4)
Variation within the Phylum
530(1)
The Noncoding Regions
531(1)
Base Composition
532(3)
The Evolution of Mitochondrial DNA in Mammals
535(9)
Phylogenetic Reconstructions
538(2)
The D-Loop Region
540(4)
The Evolution of the Human Mitochondrial Genome
544(4)
References
548(5)
Nuclear Transcription Factors in Cytochrome c and Cytochrome Oxidase Expression
553(40)
Richard C. Scarpulla
Nuclear and Mitochondrial Contributions to Respiratory Chain Expression
553(1)
Regulated Expression of Cytochrome c and Cytochrome Oxidase
554(6)
Cytochrome c Gene Expression
555(2)
Cytochrome Oxidase Gene Expression
557(3)
Activators and Repressors of Cytochrome c Gene Transcription
560(12)
Positive and Negative Regulators of Cytochrome c in Yeast
560(3)
Transcriptional Activators of Cytochrome c Expression in Mammalian Cells
563(9)
Transcriptional Activators and Repressors of Cytochrome Oxidase Gene Expression
572(7)
Activators and Repressors of Yeast Cytochrome Oxidase Genes
572(1)
Transcriptional Activators of Cytochrome Oxidase Expression in Mammalian Cells
573(6)
Perspective and Summary
579(3)
References
582(11)
Suppressor Genetics of the Mitochondrial Energy Transducing System: The Cytochrome bc1 Complex
593(28)
Jean-Paul di Rago
Piotr P. Slonimski
Introduction
593(1)
The Cytochrome bc1 Complex
594(2)
Cytochrome b Inhibitor-Resistant Mutants
596(6)
Cytochrome b Nonfunctional Missense Mutants
602(1)
Intragenic Second-Site Suppressors of Cytochrome b Nonfunctional Mutants
603(4)
Cytochrome b Frameshift Mutants and Their Revertants
607(1)
Extragenic and Intergenomic Suppressor Mutations as a Tool for the Study of Polypeptide Subunit Interactions within the Cytochrome bc1 Complex
608(5)
A Missense Point Mutation in the Nuclear Rieske Protein Gene Compensates for Functional Defects due to a Mutation in the Mitochondrial Cytochrome b Gene
608(2)
A Point Mutation in the Mitochondrial Cytochrome b Gene Obviates the Requirement of the Nuclear-Encoded Core Protein 2 Subunit in the Cytochrome bc1 Complex in
610(3)
S. cerevisiae
References
613(8)
Tissue-Specific Expression of Cytochrome c Oxidase Isoforms and Role in Nonshivering Thermogenesis
621(14)
Bernhard Kadenbach
Viola Frank
Dietmar Linder
Susanne Arnold
Stefan Exner
Maik Huttemann
Introduction
621(1)
Subunit Structure and Isoforms of Cytochrome c Oxidase
622(1)
Cytochrome c Oxidase from Turkey
623(1)
cDNAs of Subunit VIa of Trout Liver and Carp Heart
624(2)
Binding of ATP and ADP to Cytochrome c Oxidase
626(1)
Decrease of H+/e- Stoichiometry in Cytochrome c Oxidase at High Intraliposomal ATP/ADP-Ratios
627(2)
Variation of H+/e- Stoichiometry and Nonshivering Thermogenesis
629(2)
References
631(4)
Mitochondrial DNA Mutations and Nuclear Mitochondrial Interactions in Human Disease
635(30)
H. Cock
J.-W. Taanman
A. H. V. Schapira
Introduction
635(1)
Nuclear Genes in Leber's Hereditary Optic Neuropathy
636(11)
Segregation Analysis in LHON Families
638(1)
Linkage Analysis in LHON
639(1)
Mitochondrial Transfer Studies in LHON
640(4)
Nuclear Genes and Mitochondrial Dysfunction in Hutchinson--Gilford Progeria Syndrome
644(3)
Nuclear--Mitochondrial Interactions
647(9)
Autosomal Dominant Progressive External Ophthalmoplegia
647(1)
Other Mitochondrial Disorders Associated with Multiple Deletions of mtDNA
648(2)
The Etiology of Multiple mtDNA Deletions
650(2)
mtDNA Depletion Syndrome
652(1)
The Etiology of mtDNA Depletion Syndrome
653(3)
References
656(9)
Strategy toward Gene Therapy of Mitochondrial DNA Disorders
665(12)
Peter Seibel
Martina Schliebs
Adrian Flierl
Introduction
665(2)
Treatment of OXPHOS Defects
667(5)
Current Approaches
667(1)
Somatic Gene Therapy Approaches for mtDNA Diseases
668(4)
Outlook
672(1)
References
673(4)
The F0F1-ATP Synthase in Cell Proliferation and Aging
677(16)
Ferruccio Guerrieri
Introduction
677(1)
Age-Related Changes of Mitochondrial F0F1-ATP Synthase
678(3)
Possible Involvement of ROS in Age-Related Alterations of Mitochondrial F0F1-ATP Synthase
681(2)
Mitochondrial Energy Metabolism during Liver Regeneration
683(2)
Possible Involvement of ROS in the Alteration of Mitochondrial F0F1-ATP Synthase during the Early Phase of Liver Regeneration
685(3)
Concluding Remarks
688(1)
References
689(4)
Age-Linked Changes in the Genotype and Phenotype of Mitochondria
693(36)
Maria N. Gadaleta
Bernhard Kadenbach
Angela M. S. Lezza
Annette Reith
Palmiro Cantatore
Domenico Boffoli
Sergio Papa
Introduction
693(1)
The Mitochondrial Genetic System
694(5)
The mtDNA
694(3)
Characteristics of the Mitochondrial Genetic System
697(2)
The Mitochondrial OXPHOS System and Aging
699(6)
mtDNA and Aging
705(9)
mtDNA Expression and Aging
714(4)
Conclusions
718(1)
References
719(10)
Nucleus-Driven Lesions of mtDNA and Disorders of Nucleus-Encoded Energy Genes
729(22)
Massimo Zeviani
Vittoria Petruzzella
Monica Munaro
Francesca Forti
Introduction
729(1)
Nucleus-Driven Mutations of mtDNA
730(9)
Qualitative Abnormalities: Multiple Familial mtDNA Deletions
730(5)
Quantitative Abnormalities: mtDNA Depletion
735(2)
Nucleus-Driven mtDNA Mutations: Search for Candidate Genes
737(2)
Nuclear Genes and OXPHOS Disorders: Cellular Models
739(5)
``Customized'' Cybrids Using Patient-Derived rho0 Cells
740(1)
Patient/143B.rho0 Hybrids
740(2)
COX(-) LS: How Many Genes?
742(2)
Conclusions
744(2)
References
746(5)
Aging and Degenerative Diseases: A Mitochondrial Paradigm
751(22)
Douglas C. Wallace
Introduction
751(1)
Mitochondrial Bioenergetics
752(1)
mtDNA Genetics and Disease
753(1)
mtDNA Variation in Human Populations
754(2)
African mtDNA Variation
754(1)
European mtDNA Variation
755(1)
Asian mtDNA variation
755(1)
Native American mtDNAs
756(1)
mtDNA Mutations and Degenerative Disease
756(10)
Diseases Resulting from Missense Mutations
756(3)
Diseases Resulting from Protein Synthesis Mutations
759(3)
Diseases Resulting from Rearrangement Mutations
762(1)
Induction of OXPHOS Gene Expression in Mutant Tissues
762(1)
Somatic mtDNA Mutations and the Age-Related Decline of OXPHOS
762(1)
Mitochondrial Defects in Common Degenerative Diseases
763(1)
Mitochondrial Defects in Degenerative Diseases and Aging
764(2)
References
766(7)
Perspectives on the Permeability Transition Pore, a Mitochondrial Channel Involved in Cell Death
773(24)
Paolo Bernardi
Introduction
773(3)
Chemiosmosis and Mitochondrial Channels
774(1)
The Permeability Transition: Lipid or Protein?
775(1)
Mechanistic Aspects of Pore Regulation
776(4)
Matrix pH
776(1)
Membrane Potential
777(1)
Divalent Cations
778(1)
Oxidative Stress
778(1)
CsA and Cyclophilin
779(1)
Molecular Nature of the Pore: An Open Question
780(1)
The Permeability Transition Pore: A Role in Calcium Homeostasis?
781(2)
Mitochondria in Cell Death
783(4)
Necrosis
784(1)
Apoptosis
785(2)
Conclusions and Perspectives
787(1)
References
788(9)
Author Index 797(2)
Subject Index 799

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