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Energy Transduction Mechanisms (Animals and Plants)

Vladimir Skulachev

10.1002/cphy.cp140104

Source: Supplement 31: Handbook of Physiology, Cell Physiology

Originally published: 1997

Published online: January 2011

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 The Animal Cell
1.1 General Pattern of the Energy Transductions
1.2 Substrate‐Level Phosphorylations
1.3 Respiratory Chain
1.4 H+‐ATP‐Synthase and H+‐ATPases
1.5 Na+/K+‐ATPase and Ca2+‐ATPase
1.6 Δμ̅H+ and Δμ̅Na+‐Driven Transports of Solutes
1.7 H+‐Nicotinamide Nucleotide‐Transhydrogenase
1.8 Δμ̅H+ as an Energy Source for Heat Production
1.9 Intracellular Power Transmission
2 The Plant Cell
2.1 General Pattern of the Energy Transductions
2.2 Photoredox Chain
2.3 H+‐ATP‐Synthase, H+‐ATPases and H+‐Pyrophosphatase
3 Conclusion
Figure 1. Figure 1.

ΔΨ (A) and ΔpH (B) between two compartments separated by a membrane (vertical septum).
Figure 2. Figure 2.

Localization of the energy transduction processes in the animal cell, (1) Respiratory chain pumps H+ from mitochondria. (2) H+ comes back performing chemical work (ATP synthesis) or “osmotic work” (uphill transport of metabolites). (3) ATP is formed by glycolysis. (4) Chemical, “osmotic,” and mechanical work is driven by ATP hydrolysis. (5) Na+ is extruded from the cell by Na+/K+‐ATPase. (6) Na+ comes into the cell via Na+, solute‐symporters of the outer cell membrane. (7) H+ is pumped to the secretory granules, lysosomes, etc. by H+‐ATPase of vacuolar type. (8) The H+ efflux from these vesicles supports “osmotic work.”
Figure 3. Figure 3.

Energy‐yielding metabolic pathways of the animal cell. 1–6, glycolysis (3‐PGA, 2‐PGA and PEP, 3‐phosphoglyceraldehyde, 2‐phosphoglycerate and phosphoenolpyruvate, respectively); 7, oxidative decarboxylation of pyruvate; 8–14, the citric acid cycle; 15, lipolysis of the neutral fat; 16, glycerol phosphorylation and oxidation; 17–19, β‐oxidation of fatty acid (R, remainder of the fatty acid hydrocarbon chain); 20, proteolysis; 21, conversion of various amino acids to pyruvate, acetyl CoA and the citric acid cycle intermediates; 22–24, the respiratory chain; 25, reduction of CoQ by FADH2 produced in reactions 12 and 17; 26, ATP formation by H+‐ATP‐synthase. Energy transductions, namely formation of or high‐energy ATP precursors takes place at stages 3, 4, 11, 22, 23, and 24.
Figure 4. Figure 4.

Glycolytic substrate‐level phosphorylations. E, remainder of glyceraldehyde 3‐phosphate dehydrogenase; ‐SH and B, Cys‐149 and His‐176 of this enzyme.
Figure 5. Figure 5.

Phosphorylation coupled to the oxidative decarboxylation of α‐ketoglutarate. TPT, thiamine pyrophosphate; L, remainder of lipoate; E, succinate thiokinase.
Figure 6. Figure 6.

Respiratory chain of mitochondria. AH2, A respiratory substrate; FeS11,2,3,4, corresponding iron‐sulfur centers of NADH‐CoQ reductase; bb and bb high‐ and low‐potential hemes of cytochrome b; FeSIII, iron‐sulfur protein of the complex III; c1, c, a, and a3, corresponding cytochromes.
Figure 7. Figure 7.

Electron microscopic analysis of single NADH‐CoQ reductase molecule from Neurospora crassa and its hydrophobic membranous fraction, (a) The average particle of the whole enzyme; (b) an average of the hydrophobic fraction; (c) the averaged particle of the whole enzyme superimposed by the averaged particle of the hydrophobic fraction. Bar, 20 nm. It is assumed that the hydrophobic subcomplex is plugged through the membrane whereas the hydrophilic subcomplex is protruded to the mitochrondrial matrix space

From Weiss et al. 208 with permission
Figure 8. Figure 8.

Projections of CoQH2‐cytochrome c reductase reconstructed by means of an electron microscopic study of membrane crystals. The white horizontal section represents the membrane bilayer, the upper dark area the matrix space of mitochondria and the lower dark area the intermembrane space

From Leonard et al. 105 with permission
Figure 9. Figure 9.

Structure of cyochrome c from tuna muscle mitochondria. Heme and its ligands are shown by black lines

From Salamma 160 with permission
Figure 10. Figure 10.

The X‐ray structure of bovine cytochrome c oxidase at 2.8 Å resolution. Schematic representation of metal and heme location

From Tsukihara et al. 195 with permission
Figure 11. Figure 11.

The negative staining of the inside‐out submitochrondrial vesicles. As can be seen, there are numerous knobs on the outer side of the membrane. These knobs are factors F1 of H+‐ATP synthase, protruding from the membrane (negative staining, electron microphotograph by L. E. Bakeeva).
Figure 12. Figure 12.

The structure of isolated beef heart mitochondrial factor F1. Final result of the image analysis of 379 projections of negatively stained F1 molecules

From Boekema et al. 19 with permission
Figure 13. Figure 13.

H+‐ATP synthase mechanism: translocation of two or three hydrogen ion (nH+) via F0 results in a conformation change in F1 which facilitates the release of the tightly‐bound ATP from the F1 catalytic site. Hydrogen ions passing F0 are not involved in H2O formation accompanying the ATP synthesis from ADP and Pi.
Figure 14. Figure 14.

Mitochondrial—cytosolic relationships: the transport cascade of the inner mitochondrial membrane. Respiratory chain pumps H+ from the matrix (1). , H+ symporter (2) and ADP3−/ATP4− antiporter (3) mediate the influx of and ADP and the efflux of ATP. /malate2− antiport (4) results in malate influx. Malate2−/(citrate3− + H+) antiport (5) gives rise to citrate accumulation in the matrix

After Pedersen and Wehrle, 142 with permission
Figure 15. Figure 15.

Mitochondria revealed in a living human fibroblast by means of the penetrating fluorescent cation ethylrhodamine

Photograph by D. B. Zorov
Figure 16. Figure 16.

A–E. Illumination by a narrow laser beam of a small part of mitochondrial filament results in ΔΨ collapse over the entire filament length. A cell of the primary culture of human fibroblasts was stained with ethylrhodamine, before (A) and after (B‐E) 100‐ms laser treatment. The laser light spot was commensurate with the mitochondrial filament thickness. A, B, Fluorescent microscopy. C, Phase‐contrast microscopy. D, the top view on model mitochondria in the fibroblast, reconstituted with the use of the serial section technique. Arrows show the place illuminated by laser. E, Electron microscopy; a part of the laser‐treated mitochondrion is seen

From Amchenkova et al. 1 with permission
Figure 17. Figure 17.

De‐energization of filamentous mitochondrion (fibroblast) or mitochondrial cluster (heart muscle cell) induced by local damage of the mitochondrial membrane. In the latter case, it is assumed that the mitochondrial junctions are H+ permeable.

From Skulachev, 180 with permission
Figure 18. Figure 18.

General pattern of the energy transductions in the plant cell. (1) Photoredox chain pumps H+ to the thylakoid interior. (2) H+‐ATP‐synthase forms ATP, which is coupled to the downhill H+ efflux from thylakoid. (3) H+ is pumped from the mitochondrial matrix space by the respiratory chain. (4) Downhill H+ influx to matrix is coupled to ATP synthesis or to performance and “osmotic” work (for example, uptake of solutes by mitochondria via H+, solute‐symporters). (5) ATP is formed by glycolysis. (6) ATP is utilized to perform chemical, “osmotic,” and mechanical work. (7) ATP is hydrolyzed by the plasma membrane H+‐ATPase which pumps H+ from the cell. (8) Downhill H+ movement supports “osmotic” work of the outer cell membrane. (9) Na+ is pumped from the cell by Na+/H+‐antiporter. (10) H+ is pumped to vacuole by the tonoplast H+‐ATPase. (11) Downhill H+ efflux from vacuole supports “osmotic” work.

From Skulachev, 182 with permission
Figure 19. Figure 19.

The non‐cyclic photosynthetic redox chain of chloroplasts. Tyrz, tyrosine‐161, electron donor of the photosystem II; Chl680, chlorophyll of the photosystem II; Pheo, pheophytin; PQA and PQB, plastoquinones bound to photosystem II; PQ, plastoquinone pool; bh and bh high‐ and low‐potential hemes of cytochrome b6; FeSIII iron‐sulfur cluster of b6f complex; f, cytochome f; PC, plastocyanin; Chl700 and Chl693, chlorophylls of photosystem I; FeSx, the primary stable electron acceptor of photosystem I; FeSA and FeSB, two iron‐sulfur clusters tightly bound to the photosystem I; Fd, ferredoxin.
Figure 20. Figure 20.

A tentative scheme of the photosystem I reaction center complex. 83, 82, 22, 19, and 9 kD, subunits of corresponding molecular masses; PC, water‐soluble protein plastocyanin; (Chl700)2 and Chl693, the photosystem I chlorophyll dimer and monomer, respectively; K1, tightly bound vitamin K1 (phylloquinone); FeSx, the 4Fe‐4S cluster operating as the primary stable electron acceptor; FeSB and FeSA, the 4Fe‐4S clusters taking part in the electron transfer from FeSx to Fd; Fd, water‐soluble protein ferredoxin containing 2Fe‐2S clusters; arrows, the electron transfer pathway.

Adapted from Knaff 91 with permission
Figure 21. Figure 21.

A tentative scheme of the photosystem II reaction center complex. 56, 52, 39.5, 39, 33, 23, 17, 9, and 4.5 kD, subunits of corresponding molecular mass; (Chl680)2 and Chl680, the photosystem II chlorophyll dimer and monomer, respectively; Pheo, pheophytin; PQA and PQB, bound plastoquinones; arrows, the electron transfer pathway

Adapted from Rutherford 155 with permission


Figure 1.

ΔΨ (A) and ΔpH (B) between two compartments separated by a membrane (vertical septum).



Figure 2.

Localization of the energy transduction processes in the animal cell, (1) Respiratory chain pumps H+ from mitochondria. (2) H+ comes back performing chemical work (ATP synthesis) or “osmotic work” (uphill transport of metabolites). (3) ATP is formed by glycolysis. (4) Chemical, “osmotic,” and mechanical work is driven by ATP hydrolysis. (5) Na+ is extruded from the cell by Na+/K+‐ATPase. (6) Na+ comes into the cell via Na+, solute‐symporters of the outer cell membrane. (7) H+ is pumped to the secretory granules, lysosomes, etc. by H+‐ATPase of vacuolar type. (8) The H+ efflux from these vesicles supports “osmotic work.”



Figure 3.

Energy‐yielding metabolic pathways of the animal cell. 1–6, glycolysis (3‐PGA, 2‐PGA and PEP, 3‐phosphoglyceraldehyde, 2‐phosphoglycerate and phosphoenolpyruvate, respectively); 7, oxidative decarboxylation of pyruvate; 8–14, the citric acid cycle; 15, lipolysis of the neutral fat; 16, glycerol phosphorylation and oxidation; 17–19, β‐oxidation of fatty acid (R, remainder of the fatty acid hydrocarbon chain); 20, proteolysis; 21, conversion of various amino acids to pyruvate, acetyl CoA and the citric acid cycle intermediates; 22–24, the respiratory chain; 25, reduction of CoQ by FADH2 produced in reactions 12 and 17; 26, ATP formation by H+‐ATP‐synthase. Energy transductions, namely formation of or high‐energy ATP precursors takes place at stages 3, 4, 11, 22, 23, and 24.



Figure 4.

Glycolytic substrate‐level phosphorylations. E, remainder of glyceraldehyde 3‐phosphate dehydrogenase; ‐SH and B, Cys‐149 and His‐176 of this enzyme.



Figure 5.

Phosphorylation coupled to the oxidative decarboxylation of α‐ketoglutarate. TPT, thiamine pyrophosphate; L, remainder of lipoate; E, succinate thiokinase.



Figure 6.

Respiratory chain of mitochondria. AH2, A respiratory substrate; FeS11,2,3,4, corresponding iron‐sulfur centers of NADH‐CoQ reductase; bb and bb high‐ and low‐potential hemes of cytochrome b; FeSIII, iron‐sulfur protein of the complex III; c1, c, a, and a3, corresponding cytochromes.



Figure 7.

Electron microscopic analysis of single NADH‐CoQ reductase molecule from Neurospora crassa and its hydrophobic membranous fraction, (a) The average particle of the whole enzyme; (b) an average of the hydrophobic fraction; (c) the averaged particle of the whole enzyme superimposed by the averaged particle of the hydrophobic fraction. Bar, 20 nm. It is assumed that the hydrophobic subcomplex is plugged through the membrane whereas the hydrophilic subcomplex is protruded to the mitochrondrial matrix space

From Weiss et al. 208 with permission


Figure 8.

Projections of CoQH2‐cytochrome c reductase reconstructed by means of an electron microscopic study of membrane crystals. The white horizontal section represents the membrane bilayer, the upper dark area the matrix space of mitochondria and the lower dark area the intermembrane space

From Leonard et al. 105 with permission


Figure 9.

Structure of cyochrome c from tuna muscle mitochondria. Heme and its ligands are shown by black lines

From Salamma 160 with permission


Figure 10.

The X‐ray structure of bovine cytochrome c oxidase at 2.8 Å resolution. Schematic representation of metal and heme location

From Tsukihara et al. 195 with permission


Figure 11.

The negative staining of the inside‐out submitochrondrial vesicles. As can be seen, there are numerous knobs on the outer side of the membrane. These knobs are factors F1 of H+‐ATP synthase, protruding from the membrane (negative staining, electron microphotograph by L. E. Bakeeva).



Figure 12.

The structure of isolated beef heart mitochondrial factor F1. Final result of the image analysis of 379 projections of negatively stained F1 molecules

From Boekema et al. 19 with permission


Figure 13.

H+‐ATP synthase mechanism: translocation of two or three hydrogen ion (nH+) via F0 results in a conformation change in F1 which facilitates the release of the tightly‐bound ATP from the F1 catalytic site. Hydrogen ions passing F0 are not involved in H2O formation accompanying the ATP synthesis from ADP and Pi.



Figure 14.

Mitochondrial—cytosolic relationships: the transport cascade of the inner mitochondrial membrane. Respiratory chain pumps H+ from the matrix (1). , H+ symporter (2) and ADP3−/ATP4− antiporter (3) mediate the influx of and ADP and the efflux of ATP. /malate2− antiport (4) results in malate influx. Malate2−/(citrate3− + H+) antiport (5) gives rise to citrate accumulation in the matrix

After Pedersen and Wehrle, 142 with permission


Figure 15.

Mitochondria revealed in a living human fibroblast by means of the penetrating fluorescent cation ethylrhodamine

Photograph by D. B. Zorov


Figure 16.

A–E. Illumination by a narrow laser beam of a small part of mitochondrial filament results in ΔΨ collapse over the entire filament length. A cell of the primary culture of human fibroblasts was stained with ethylrhodamine, before (A) and after (B‐E) 100‐ms laser treatment. The laser light spot was commensurate with the mitochondrial filament thickness. A, B, Fluorescent microscopy. C, Phase‐contrast microscopy. D, the top view on model mitochondria in the fibroblast, reconstituted with the use of the serial section technique. Arrows show the place illuminated by laser. E, Electron microscopy; a part of the laser‐treated mitochondrion is seen

From Amchenkova et al. 1 with permission


Figure 17.

De‐energization of filamentous mitochondrion (fibroblast) or mitochondrial cluster (heart muscle cell) induced by local damage of the mitochondrial membrane. In the latter case, it is assumed that the mitochondrial junctions are H+ permeable.

From Skulachev, 180 with permission


Figure 18.

General pattern of the energy transductions in the plant cell. (1) Photoredox chain pumps H+ to the thylakoid interior. (2) H+‐ATP‐synthase forms ATP, which is coupled to the downhill H+ efflux from thylakoid. (3) H+ is pumped from the mitochondrial matrix space by the respiratory chain. (4) Downhill H+ influx to matrix is coupled to ATP synthesis or to performance and “osmotic” work (for example, uptake of solutes by mitochondria via H+, solute‐symporters). (5) ATP is formed by glycolysis. (6) ATP is utilized to perform chemical, “osmotic,” and mechanical work. (7) ATP is hydrolyzed by the plasma membrane H+‐ATPase which pumps H+ from the cell. (8) Downhill H+ movement supports “osmotic” work of the outer cell membrane. (9) Na+ is pumped from the cell by Na+/H+‐antiporter. (10) H+ is pumped to vacuole by the tonoplast H+‐ATPase. (11) Downhill H+ efflux from vacuole supports “osmotic” work.

From Skulachev, 182 with permission


Figure 19.

The non‐cyclic photosynthetic redox chain of chloroplasts. Tyrz, tyrosine‐161, electron donor of the photosystem II; Chl680, chlorophyll of the photosystem II; Pheo, pheophytin; PQA and PQB, plastoquinones bound to photosystem II; PQ, plastoquinone pool; bh and bh high‐ and low‐potential hemes of cytochrome b6; FeSIII iron‐sulfur cluster of b6f complex; f, cytochome f; PC, plastocyanin; Chl700 and Chl693, chlorophylls of photosystem I; FeSx, the primary stable electron acceptor of photosystem I; FeSA and FeSB, two iron‐sulfur clusters tightly bound to the photosystem I; Fd, ferredoxin.



Figure 20.

A tentative scheme of the photosystem I reaction center complex. 83, 82, 22, 19, and 9 kD, subunits of corresponding molecular masses; PC, water‐soluble protein plastocyanin; (Chl700)2 and Chl693, the photosystem I chlorophyll dimer and monomer, respectively; K1, tightly bound vitamin K1 (phylloquinone); FeSx, the 4Fe‐4S cluster operating as the primary stable electron acceptor; FeSB and FeSA, the 4Fe‐4S clusters taking part in the electron transfer from FeSx to Fd; Fd, water‐soluble protein ferredoxin containing 2Fe‐2S clusters; arrows, the electron transfer pathway.

Adapted from Knaff 91 with permission


Figure 21.

A tentative scheme of the photosystem II reaction center complex. 56, 52, 39.5, 39, 33, 23, 17, 9, and 4.5 kD, subunits of corresponding molecular mass; (Chl680)2 and Chl680, the photosystem II chlorophyll dimer and monomer, respectively; Pheo, pheophytin; PQA and PQB, bound plastoquinones; arrows, the electron transfer pathway

Adapted from Rutherford 155 with permission
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Article Title: Energy Transduction Mechanisms (Animals and Plants)
 

How to Cite

Vladimir Skulachev. Energy Transduction Mechanisms (Animals and Plants). Compr Physiol 2011, Supplement 31: Handbook of Physiology, Cell Physiology: 76-116. First published in print 1997. doi: 10.1002/cphy.cp140104