Higher Plant Cell Respiration

538 Pages·1985·11.7 MB·English

by  D. A. Day

Encyclopedia of
Plant Physiology
New Series Volume 18
Editors
A. Pirson, G6ttingen
M.H. Zimmermann, Harvard
Higher Plant Cell
Respiration
Edited by
R. Douce and D.A. Day
Contributors
T.ap Rees M. Chauveau S. Delorme P. Dizengremel
I.B. Dry G. Ducet G.E. Edwards D. Fa1conet P. Gardestr6m
lB. Hanson 11. Harwood H. Lambers C. Lance B. Lejeune
C.A. Mannella A.L. Moore M. Neuburger 1M. Palmer
F. Quetier P.R Rich M. Steup M. Stitt lA. Ward
1 T. Wi skich
With a Foreword by H. Beevers
Springer-Verlag
Berlin Heidelberg NewY ork Tokyo
Dr. ROLAND DOUCE
Centre d' Etudes Nucleaires et Universite Scientifique
et Medicale de Grenoble
Departement de Recherche Fondamentale
Laboratoire de Physiologie Cellulaire Vegetale
UA CNRS N° 576
85X
F-38041 Grenoble Cedex
France
Dr. DAVID A. DAY
Botany Department
The Australian National University
Box 475 P.O.
Canberra City, ACT 2601
Australia
With 81 Figures
ISBN-13: 978-3-642-70103-0 e-ISBN-13: 978-3-642-70101-6
001: 10.1007/978-3-642-70101-6
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Foreword
I am honored by the editor's invitation to write a Preface for this volume.
As a member of an older generation of plant physiologists, my lineage in plant
respiration traces back to F.F. BLACKMAN through the privilege of having
M. THOMAS and W.O. JAMES, two of his "students," as my mentors. How the
subject has changed in 40 years!
In those dark ages B. 14C. most of the information available was hard-won
from long-term experiments using the input-output approach. Respiratory
changes in response to treatments were measured by laborious gas analysis
or by titration of alkali from masses of Pettenkofer tubes; the Warburg respir
ometer was just beginning to be used for plant studies by pioneers such as
TURNER and ROBERTSON. Nevertheless the classical experiments of BLACKMAN
with apples had led to important results on the relations between anaerobic
and aerobic carbohydrate utilization and on the climacteric, and to the first
explicit concept of respiratory control of respiration imposed by the" organiza
tion resistance" of cell structure. THOMAS extended this approach in his investi
gations of the Pasteur effect and the induction of aerobic fermentation by poi
sons such as cyanide and high concentrations of CO2, JAMES began a long
series of studies of the partial reactions of respiration in extracts from barley
and YEMM'S detailed analysis of carbohydrate components in relation to respira
tory changes added an important new dimension. Much emphasis was placed
on the soluble oxidases, phenol oxidase, ascorbate oxidase, and peroxidase,
those distinctive plant enzymes which seemed so inevitably associated with their
respiration. The work of HILL, GODDARD, and OKUNUKI on the plant cyto
chromes refocused attention to where it belonged, as expected from considera
tions of comparative biochemistry. JAMES' important book on Plant Respiration
was an authoritative survey of the achievements up to 1953, and the various
editions of Plant Physiology by Thomas and his colleagues provided extensive
coverage of this subject.
The early 1950's saw a transition in the study of plant respiration that
was shared by most other fields of biological research. The increasing availability
of research funds, more sophisticated instruments, labeled substrates, coenzymes
and other biochemicals, were major contributing factors. The investigation of
plant respiration proceeded along several lines. The new instruments, 02-elec
trodes, and infra-red analyzers allowed rapid and continuous recording of gas
exchanges and the Warburg and other respirometers became generally available.
High speed centrifuges allowed the separation of organelle fractions, and spectro
photometers made possible precise investigations of individual enzyme reactions.
The enzymatic reactions of glycolysis were firmly established during this
period, and mitochondria from plants, first isolated from mung bean by BON
NER'S group at Caltech in 1950, became the focus of attention from many groups
around the world. The work of LATIES and others established the central impor-
VI Foreword
tance of the TCA cycle in plant respiration. In retrospect it is ironic that many
of the acids were first discovered in plants long before they were so elegantly
enshrined in the TCA cycle by KREBS. Cyanide-resistant respiration in plant
tissues and mitochondria engaged attention, and AXELROD'S investigations led
to the establishing of the oxidative pentose phosphate pathway as a constitutive
part of respiration in plants. Volume XII of the first edition of the Encyclopedia,
edited by J. WOLF, appeared in 1960 and dealt comprehensively with Plant Respi
ration in over 2000 pages, and my own book on Respiratory Metabolism in
1961 summarized these developments rather mOre briefly. By that time the
dual role of respiration in providing intermediates for all kinds of synthetic
reactions, as well as the reducing equivalents and A TP required for their ac
complishment, had been demonstrated, although not precisely quantified. The
overall rate of normal respiration had been shown to be due not to the limited
capacity of some key enzymatic reaction, but was governed instead by intracellu
lar control mechanisms. The ways in which the pace of reactions driven by
respiration determined its rate, and particularly the role of ATP turnover in
the control of aerobic and anaerobic respiration were being recognized.
Since that time many of the respiratory enzymes have been prepared in
highly purified form by TURNER and others, and much has been learned about
the details of regulation imposed by allosteric effectors. Progress has been forth
coming on the mechanisms underlying respiratory changes in aging of tissue
slices and in ripening. Purified mitochondria, those marvelous machines of ATP
generation, have been intensively investigated and the discussion of the many
aspects of this subject occupy, appropriately, a large part of the present volume.
The discovery of photo respiration and the role of organelles, including mito
chondria in this process, was not anticipated in 1960. The impressive progress
recorded in this volume concerning all aspects of the biochemistry of plant
respiration has made possible the investigation of linked processes such as ion
and metabolite transport within and between cells, and more definitive estimates
of the respiratory costs of dependent processes in the life of the plant. The
efficiency with which respiratory breakdown of carbohydrate is linked with
synthesis of cell constituents, and with repair and maintenance of cell structures
is now being investigated, and models indicating how respiratory energy is ap
portioned to various functions have been generated.
These developments in the understanding of the biochemical and physiologi
cal aspects of plant respiration represent important achievements since the cover
age on the topic in the first edition of the Encyclopedia. The authors of the
various chapters in the present volume are among those who have contributed
most significantly, and appropriately reflect the present international character
of research on this important subject. We can only marvel at the progress
that has been made and wonder what new developments the next 20 years
will bring. Certainly the questions now being asked are very different from
those that intrigued us 40 years ago, when even the main pathways were not
established. A major challenge now is to understand more precisely how the
process of respiration is regulated and integrated into the overall functioning
of the plant as a whole.
HARRY BEEVERS
Biology Department
University of California, Santa Cruz
Contents
Introduction
DA DAY and R. DOUCE (With 1 Figure)
1 Preparation of Plant Mitochondria, Criteria for Assessement of Mitochon
drial Integrity and Purity, Survival in Vitro
M. NEUBURGER (With 8 Figures)
1 Introduction . . . . . . . . . . . . . . . . . . . . . . 7
2 General Considerations for the Isolation of Intact Mitochondria 7
3 Large-Scale Preparation of Washed Mitochondria 9
3.1 Reagents . . . . . . . . . . . . . . . . . . . . . . 9
3.2 Procedure for Potato Tuber Mitochondria ....... 10
4 Assessment of Mitochondrial Integrity . . . . . . . . . . . 10
4.1 Spectrophotometric Assay for Succinate: Cytochrome c Oxidoreductase 10
4.2 KCN-Sensitive-Ascorbate-Cytochrome c-Dependent O Uptake 11
2
5 Control of Mitochondrial Purity 12
6 Purification of Plant Mitochondria 13
6.1 Purification on Sucrose Gradients 13
6.2 Purification on Percoll Gradients 14
6.2.1 Purification of Mitochondria from Potato Tubers 15
6.2.2 Purification of Mitochondria from Pea Leaves 16
6.2.3 Properties of Percoll-Purified Mitochondria 19
7 Concluding Remarks 21
References .................... 22
2 Molecular Organization and Expression of the Mitochondrial Genome
of Higher Plants
F. QUETIER, B. LEJEUNE, S. DELORME, and D. FALCONET (With 3 Figures)
1 Introduction . . . . . . . . . . . . 25
2 Physicochemical Characterization . . . . . . . . . . . . . . . 26
2.1 Buoyant Density and Melting Point ............ 26
2.2 Direct Observation ofmtDNA Molecules by Electron Microscopy 26
2.3 Cot Curves and Kinetic Complexity ............. 27
2.4 Detection of Discrete Circular mtDNA Molecules by Gel Electrophoresis 27
3 Restriction Analysis and Molecular Cloning 28
3.1 Restriction Patterns 28
3.2 Molecular Cloning 29
3.3 Physical Map(s) ofmtDNA 29
4 Identified Mitochondrial Genes 32
4.1 rRNA Genes 32
4.2 tRNA Genes . . 33
4.3 Protein Genes 33
5 Concluding Remarks 33
References ...... 34
VIII Contents
3 Plant Mitochondrial Lipids: Structure, Function and Biosynthesis
J.L. HARWOOD (With 9 Figures)
1 Introduction to Lipid Structures . . . . . . 37
2 Composition of Mitochondrial Membranes . 39
2.1 Content of Acyl and Other Lipids . . . 39
2.2 Comparison with Other Plant Membranes 43
3 Metabolism ............. . 45
3.1 Sources of Precursors for Lipid Synthesis 45
3.2 Mitochondrial Phospholipid Synthesis 47
3.3 Degradative Enzymes ..... 53
4 Functional Aspects of Lipids . . . . 56
4.1 Membrane Structure and Function 56
4.2 Changes in Mitochondrial Lipids 60
5 Conclusion 64
References .......... . 64
4 Plant Mitochondrial Cytochromes
G. DUCET (With 2 Figures)
1 Introduction . . . . . . . . . . . . . . 72
2 Cytochrome Estimation . . . . . 74
3 Mitochondrial Cytochromes in Higher Plants 77
3.1 The c Cytochromes 77
3.1.1 Cytochrome c . . . . . . 77
3.1.2 Cytochrome c1 ..•.. 78
3.2 The b Cytochromes ...... 79
3.2.1 The Various Cytochromes b 79
3.2.2 The Cytochrome b--c Complex 85
1
3.2.3 Cytochromes b of the External Mitochondrial Membrane 86
3.3 The a Cytochromes ................... 86
4 Influence of the Membrane Potential on the Redox States of the Mitochondri-
al Cytochromes . . . . . . . . . . . . . . . . . . . . . . . 93
5 Miscellany . . . . . . . . . . . . . . . . . . . . . . . . . 96
6 Cytochromes in the Respiratory Chain of Higher Plant Mitochondria 96
References .......................... 97
5 The Outer Membrane of .Plant Mitochondria
C.A. MANNELLA (With 10 Figures)
1 Perspective . . . . . . . . . . . . . . . . . . . . . 106
2 Isolation of Mitochondrial Membranes . . . . . . . . . 107
3 Lipid Composition of the Mitochondrial Outer Membrane 109
3.1 Lipid Classes . . . . . . . . . . . . . . . . 110
3.2 Fatty Acid Composition: Temperature Modulation 111
3.3 Lipid Phase Transitions ........... 112
4 Enzymes of the Mitochondrial Outer Membrane . . . 114
4.1 The NADH: Cytochrome c Oxidoreductase System. 114
4.1.1 Possible Functions of the Outer Membrane Redox Chain 116
5 Channel-Formers of the Outer Mitochondrial Membrane . . 118
5.1 Structural Evidence for the Existence of Pores . . . . . 118
5.2 Trypsin-Insensitive Polypeptides of the Plant Membrane 120
5.3 The Pore-Forming Polypeptides . . . . . 120
5.4 Structure and Function of the Channels .... .. 123
5.4.1 Model from X-ray Diffraction . . . . . . . . . 123
5.4.2 Structure from Electron Microscopy . . . . . . 125
5.4.3 Mechanism of Ion Selectivity ......... 125
5.5 Speculation on a Regulatory Role for Outer Membrane Channels 126
References ........................... 128
Contents IX
6 Organization of the Respiratory Chain and Oxidative Phosphorylation
A.L. MOORE and P.R. RICH (With 7 Figures)
1 Introduction . . . . . . . . . . . . 134
2 Organization of Respiratory Components 135
2.1 The Basic Functional Units . . . . 135
2.1.1 Complex I, NADH Dehydrogenase 136
2.1.2 Complex II, Succinate Dehydrogenase 137
2.1.3 Complex III, the Cytochrome bC Complex 138
I
2.1.4 Complex IV, Cytochrome Oxidase . 141
2.1.5 The Alternative Oxidase ..... 142
2.1.6 The External NADH Dehydrogenase 143
3 Connection Between the Functional Units 144
3.1 The Sided ness of the Reactions of the Alternative Oxidase, Succinate
Dehydrogenase and the External NADH Dehydrogenase 144
3.2 The Role of Ubiquinone as a Mobile Redox" Pool" 145
3.2.1 Mobility Between Components ........ 145
3.2.2 The Role of Ubiquinone in Providing Mobility . . 146
3.2.3 The Relation of the Quinone Pool to Control of Electron Flow
Through the Cytochrome and Alternative Oxidases . . . 147
3.3 Some Instances Where Ideal Q-Pool Behaviour Is Not Observed 148
4 Oxidative Phosphorylation . . . . . . 150
4.1 Background .......... 150
4.2 Proton Electrochemical Gradient 151
4.2.1 Steady-State Ion Distribution 151
4.2.2 Spectroscopic Probes . . . . 153
4.2.3 Ion-Specific Electrodes . . . 154
4.2.4 Magnitude of LI p and its Response to the Metabolic State 155
4.3 Mechanism for Generating LIp 155
4.3.1 H +/ 0 Ratios 155
4.3.2 H+ /Site Ratios 158
4.3.3 H+ /ATP Ratios 159
4.4 Thermodynamic Competence of LIp 160
4.5 Is LIp an Obligate Intermediate? 162
References .............. 163
7 The Oxidation of NADH by Plant Mitochondria
1.M. PALMER and 1.A. WARD
1 Introduction . . . . . . . . . . . . . . . . 173
2 NADH Dehydrogenases Oxidizing Exogenous NADH 180
2.1 The Outer Membrane NADH Dehydrogenase . . 180
2.2 The Inner Membrane NADH Dehydrogenase . . 182
2.2.1 Location of the Dehydrogenase ..... 182
2.2.2 Nature of the Redox Components and Relationship with the Re
spiratory Chain . . . . . . . . . . . . . . . . . . . . . 183
2.2.3 Inhibitors of the External Dehydrogenase . . . . . . . . . . 185
2.2.4 Specificity of the External NADH Dehydrogenase for the Nicotin
amide Adenine Dinucleotide . . . . . . . . . . . . . . . . 186
2.2.5 Regulation of Electron Flux Through the External NADH Dehy-
drogenase ....................... 188
2.2.6 The Physiological Significance of Regulation of the NADH Dehy-
drogenase ............... 190
3 NADH Dehydrogenases Oxidizing Endogenous NADH 190
3.1 Rotenone-Sensitive Oxidation of Endogenous NADH 191
3.1.1 Redox Components Associated with the Dehydrogenase 191
3.1.2 Regulation of Electron Flow Through the Rotenone-Sensitive De-
hydrogenase ...................... 192
x
Contents
3.2 Rotenone-Resistant Oxidation of Endogenous NADH ...... . 193
3.2.1 Relationship to the Terminal Oxidases . . . . . . . 194
3.2.2 Relationship to the NAD+ -Linked Krebs Cycle Dehydrogenases 195
References 196
8 The Cyanide-Resistant Pathway of Plant Mitochondria
C. LANCE, M. CHAUVEAU, and P. DrZENGREMEL (With 10 Figures)
1 Introduction 202
2 The Measure of Cyanide Resistance 203
3 The Dependence on Respiratory Substrates 205
4 The Inhibition of Electron Transport 207
4.1 Inhibitors of the Flavoprotein Pathway 208
4.2 Inhibitors of the Cytochrome Pathway 209
4.3 Inhibitors of the Alternative Pathway 210
4.4 Interactions Between Inhibitors 211
5 The Link with Energy Transduction 213
5.1 Oxidative Phosphorylation 214
5.2 Membrane Potential and Proton Gradient 215
6 The Structure of the Alternative Pathway . 216
6.1 Branch Point of the Alternative Pathway 216
6.2 Other Components 217
7 The Functional Organization of the Alternative Pathway 217
7.1 Topographical Organization 218
7.2 Compartmentation 219
7.2.1 Ubiquinone 219
7.2.2 Pyridine Nucleotides 221
7.3 Organization of the Alternative Pathway 222
8 The Alternative Pathway Oxidase 224
8.1 Flavoprotein Hypothesis 224
8.2 Excess Oxidase Hypothesis . . . 224
8.3 Cytochrome b Hypothesis . . . 225
7
8.4 Nonheme Iron Protein Hypothesis 226
8.5 Ubiquinone (Q-Cycle) Hypothesis 227
8.6 Quinol Oxidase Hypothesis 228
8.7 Lipoxygenase Hypothesis 228
8.8 Free Radical Hypothesis 228
8.9 Conclusions 230
9 The Distribution of Electrons Between the Two Pathways 230
9.1 Some Definitions and Remarks 231
9.2 Distribution of Electrons Between Pathways . 232
9.2.1 Bahr and Bonner's Method 232
9.2.2 De Troostembergh and Nyns's Method 235
9.2.3 ADP/O Ratio Method 235
9.3 Mechanism of Electron Distribution 236
10 The Biogenesis of the Alternative Pathway 236
11 The Significance of the Alternative Pathway 237
12 Conclusion 238
References 239
9 Membrane Transport Systems of Plant Mitochondria
J.B. HANSON (With 5 Figures)
1 Introduction 248
2 Structural and Osmotic Properties 249
3 Techniques of Measuring Transport 252
Contents XI
4 Transport of Inorganic Ions and Acetate 253
4.1 Background ......... 253
4.2 Mechanisms of Passive Transport 254
4.3 Energy-Linked Transport . . . . 257
4.3.1 Salt Efflux ....... 258
4.3.2 Salt Influx ....... 260
5 Transport of Organic Metabolites and Cofactors 264
5.1 General Characteristics . . . 264
5.2 Monocarboxylate Transport 265
5.3 Dicarboxylate Transport 266
5.4 Tricarboxylate Transport 269
5.5 Amino Acid Transport 270
5.6 Nucleotide Transport 272
6 Conclusions 275
References ........ 275
10 The Tricarboxylic Acid Cycle in Plant Mitochondria: Its Operation and
Regulation
J.T. WISKICH and I.B. DRY (With 8 Figures)
1 Introduction . . . . 281
2 Control . . . . . . 282
2.1 Adenylate Enery 282
2.2 Substrate Supply 285
2.3 Enzyme Activity 288
2.3.1 Enzyme Turnover 290
2.3.2 Pyruvate Dehydrogenase 290
2.3.3 Citrate Synthase . . . . 291
2.3.4 Isocitrate Dehydrogenase 291
2.3.5 Oxoglutarate Dehydrogenase 293
2.3.6 Succinyl Coenzyme A Synthetase 293
2.3.7 Succinate Dehydrogenase . . . 293
2.3.8 Fumarase ......... 294
2.3.9 Malate Dehydrogenase and Malic Enzyme 294
3 Fatty Acid Oxidation ............. 296
3.1 Glyoxysome - Mitochondria Interactions . . . 297
4 Malate Oxidation: Malate Dehydrogenase or NAD-Malic Enzyme? 300
5 Glycine Oxidation . . . . . . . . . . 303
6 Physiological Control of the TCA Cycle 307
7 List of Enzymes 308
References .............. 308
11 Leaf Mitochondria (C + C + CAM)
3 4
P. GARDESTROM and G.E. EDWARDS (With 3 Figures)
1 Introduction . . . . . . . . . . 314
2 Effects of Light on Dark Respiration 314
3 Preparation of Leaf Mitochondria . 316
3.1 Introduction . . . . . . . . 316
3.2 Development of Preparation Procedures 317
3.2.1 C Plants . . . . . . . . . 317
3
3.2.2 CAM Plants ....... 319
3.2.3 C Plants . . . . . . . . . 319
4
4 Properties of Isolated Leaf Mitochondria 320
4.1 Purity and Intactness 320
4.2 Composition . . . . . . . . . . 321