Abstract
One of the functions of science is to bring order out of chaos. At the end of the nineteenth century cyto-chaos reigned, at least in the mind of the observer. For fifty years almost every cytologist of note had reported granular thread-like particles in the cytoplasm of aerobic cells, and assigned a name and function to them—fila, chondriokonts, fädenkörner, blepharoblasts, vermicules and others. As the twentieth century progressed and a basic uniformity of function became apparent, the name mitochondrion (Benda, 1898) became generally accepted. It is now clear that, although mitochondria in different cell types may vary in biochemical details and in size, structure and frequency, they all contain the enzymes of the tricarboxylic acid cycle (TCA cycle) and carry out oxidative phosphorylation—ATP synthesis coupled to substrate oxidation. They also all conform to a basic structural pattern, namely ah outer membrane or envelope enclosing an inner membrane which has tube-like invaginations (cristae) into an inner compartment (the matrix). The cristae membrane of liver mitochondria (figure 4.1) is 3–4 times greater than the outer membrane area. Some mitochondria, particularly those from kidney, heart and skeletal muscle (figures 4.2 and 4.3), have more extensive cristae arrangements than liver mitochondria, while others (e.g. from fibroblasts, nerve axons and most plant tissues) have relatively few cristae. Mitochondria in epithelial cells of carotid bodies have only four or five cristae, and mitochondria from non-myelinated axons of rabbit brain have only a single crista. The cristae membranes are the sites of certain TCA cycle enzymes, respiratory chain components, and the enzyme, ATP synthetase; therefore, not surprisingly there is a rough correlation between the respiratory rates of mitochondria and the extent of their cristae. Typically tissues with high respiration rates have mitochondria with many cristae.
Keywords
- Cytochrome Oxidase
- Liver Mitochondrion
- NADH Dehydrogenase
- Adenylate Kinase
- Mitochondrial Protein Synthesis
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Further Reading
Boyer, P. D., Chance, B., Ernster, L., Mitchell, P., Racker, E. and Slater, E. C. (1977) Oxidative phosphorylation and photophosphorylation. Ann. Rev. Biochem. 46, 955–1026.
Mitchell, P. (1976) Vectorial chemistry and the molecular mechanisms of chemiosmotic coupling: power transmission by proticity. Biochem. Soc. Trans. 4, 399–430.
Moorman, A. F. M., Van Ommen, G-J. B. & Grivell, L. A. (1978) Transcription in yeast mitochondria: Isolation and physical mapping of messenger RNAs for subunits of cytochrome c oxidase and ATPase. Molec. gen. Genet. 160, 13–24.
Munn, E. A. (1974) The Structure of Mitochondria. Academic Press, London.
Palmer, J. M. (1976) The organisation and regulation of electron transport in plant mitochondria. Ann. Rev. Plant Physiol. 27, 133–180.
Rottenberg, H. (1975) The measurement of transmembrane electrochemical proton gradients. Bioenergetics 7, 61–74.
Slonimski, P. P. & Tzagoloff, A. (1976) Localization in yeast mitochondria DNA of mutations expressed in a deficiency of cytochrome oxidase and/or coenzyme QH2-cytochrome c reductase. Eur. J. Biochem 61, 27–41.
Literature Cited
Brand, M. D. (1979) Stoichiometry of charge and proton translocation in mitochondria. Biochem. Soc. Trans, (in press).
Chance, B. (1972) The nature of electron transfer and energy coupling reactions. FEBS Letts. 23, 3–20.
Cotl, C, Solioz, M., Schatz, G. (1979) Biogenesis of the Cytochrome bc 1 complex of Yeast Mitochondria. J. Biol. Chem. 254, 1437–1439.
Hinkle, P. C. & Wu, M. L. (1979) The phosphorus/oxygen ratio of mitochondrial oxidative phosphorylation. J. Biol. Chem. 254, 2450–2455.
Luck, D. J. L. (1963) Formation of mitochondria in Neurospora crassa. J. Cell Biol. 16, 483–499.
Maccecchim, M-L., Rudin, Y., Blobel., G. & Schatz, G. (1979) Import of proteins into mitochondria. Proc. Nat. Acad. Sci. U.S.A. 76, 343–347.
Macino, G. & Tzagoloff, A. (1979) The DNA sequence of a mitochondrial ATPase gene in Saccharomyces cerevisiae. J. Biol. Chem. 254, 4617–4623.
Mahler, H. R. (1973) Biogenetic autonomy of mitochondria. CRC Critical Reviews in Biochemistry, pp. 381–460.
Mayer, R. J. (1979) Turnover of mitochondrial proteins in rat liver. Biochem. Soc. Trans. 7, 306–310.
Mitchell, P. (1961) Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature 191, 144–147.
Mitchell, P. (1979) Compartmentation and communication in living systems. Ligand conduction: a general catalytic principle in chemical, osmotic and chemiosmotic reaction systems. Eur. J. Biochem. 95, 1–29.
Mitchell, P. & Moyle, J. (1979) Respiratory-chain protonmotive stoichiometry. Biochem. Soc. Trans, (in press).
Nass, M. M. K. & Nass, S. (1963) Intramitochondrial fibres with DNA characteristics. J. Cell Biol. 19, 613–629.
Palmer, J. M. (1979) The ‘uniqueness’ of plant mitochondria. Biochem. Soc. Trans. 7, 246–252.
Racker, E. (1975) Reconstitution, mechanism of action and control of ion pumps. Biochem. Soc. Trans. 3, 785–802.
Reid, R. A. (1974) Reversal of adenosine triphosphatase in chloroplasts and mitochondria by transmembrane ion gradients. Biochem. Soc. Spec. Publ. 4, 113–129.
Slonimski, P. P. et al. (1978) Mosaic organization and expression of the mitochondrial DNA region controlling cytochrome c reductase and oxidase. In Biochemistry and Genetics of Yeast ed. Bacila, M., Horecker, B. L. & Stoppani, A. D. M., Academic Press.
Smith, G. S. & Reid R. A. (1978) The influence of respiratory state on monoamine oxidase activity in rat liver mitochondria. Biochem. J. 176, 1011–1014.
Tzagoloff, A., Macino, G. & Sebald, W. (1979) Mitochondrial genes and translation products. Ann. Rev. Biochem. 48, 419–441.
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© 1980 R. A. Reid and R. M. Leech
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Reid, R.A., Leech, R.M. (1980). Mitochondria. In: Biochemistry and Structure of Cell Organelles. Tertiary Level Biology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-7200-4_4
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