Electron microscopy and image analysis of the complexes I and V of the mitochondrial respiratory chain.
The results of Section IV can be summarized in a simple ATP synthase model. This model implies that either the alpha or the beta subunits must be closer to the membrane. The work of Gao and Bauerlein (1987) indicates that the alpha subunits are closer to the membrane. Although the overall structure is more or less clear, important questions need to be clarified. First, the number and the arrangement of the subunits in the F0 part must be known. Second, the exact shape of F1, and particularly the shape of the large subunits needs to be elucidated. On the basis of fluorescence resonance energy transfer measurements by McCarty and Hammes (1987), a model was presented showing large oblong subunits. Such 'banana-shaped' subunits, which are also presented in the many phantasy models (e.g. Walker et al., 1982), are very unlikely in view of the electron microscopical results, although the large subunits do not need to be exactly spherical. The third and most interesting central question is on the changes in the structure that take place during the different steps in the synthesis of ATP. It can now be taken as proven that the energy transmitted to the ATP synthase is used to induce a conformational change in the latter enzyme, in such a way as to bring about the energy-requiring dissociation of already synthesized ATP (Penefsky, 1985 and reviewed in Slater, 1987). But the way in which the three parts of the ATP synthase are involved is completely unknown. It is rather puzzling that such a long distance exists between the catalytic sites, which are on the interface of the alpha and beta subunits and the F0 part where the proton movements occur, which, according to Mitchell's theory (1961), is the driving force for the synthesis of ATP. Perhaps alternative mechanisms such as the collision hypothesis formulated by Herweijer et al. (1985) are more realistic in describing the mechanism of ATP synthesis. It would bring the complexes I and V close together, not only in the artificial way treated in this paper, but in a useful way for energy conversion.
Brink
J
J
Biochemisch Laboratorium, Rijksuniversiteit Groningen, The Netherlands.
Boekema
E J
EJ
van Bruggen
E F
EF
D000818:Animals; D002417:Cattle; D003460:Crystallization; D005656:Fungal Proteins / Q000648:ultrastructure; D007091:Image Processing, Computer-Assisted; D008854:Microscopy, Electron / Q000379:methods*; D008928:Mitochondria / Q000201:enzymology* / Q000648:ultrastructure; D008929:Mitochondria, Heart / Q000201:enzymology / Q000648:ultrastructure; D025261:Mitochondrial Proton-Translocating ATPases; D008958:Models, Molecular; D016660:NAD(P)H Dehydrogenase (Quinone); D009245:NADH Dehydrogenase / Q000648:ultrastructure*; D009492:Neurospora crassa / Q000201:enzymology; D010085:Oxidative Phosphorylation; D006180:Proton-Translocating ATPases / Q000648:ultrastructure*; D011808:Quinone Reductases / Q000648:ultrastructure*
D005656:Fungal Proteins; C021983:complex V (mitochondrial oxidative phosphorylation system); D016660:NAD(P)H Dehydrogenase (Quinone); D011808:Quinone Reductases; D009245:NADH Dehydrogenase; D025261:Mitochondrial Proton-Translocating ATPases; D006180:Proton-Translocating ATPases