Summary
The matrix space of mitochondria is surrounded by two membranes. The mitochondrial inner membrane contains the respiration chain and a large number of highly specific carriers for the mostly anionic substrates of mitochondrial metabolism. In contrast to this the permeability properties of the mitochondrial outer membrane are by far less specific. It acts as a molecular sieve for hydrophilic molecules with a defined exclusion limit around 3000 Da. Responsible for the extremely high permeability of the mitochondrial outer membrane is the presence of a pore-forming protein termed mitochondrial porin. Mitochondrial porins have been isolated from a variety of eukaryotic cells. They are basic proteins with molecular masses between 30 and 35 kDa. Reconstitution experiments define their function as pore-forming components with a single-channel conductance of about 0.40 nS (nano Siemens) in 0.1 M KCl at low voltages. In the open state mitochondrial porin behaves as a general diffusion pore with an effective diameter of 1.7 nm. Eukaryotic porins are slightly anion-selective in the open state but become cation-selective after voltage-dependent closure.
Similar content being viewed by others
References
Benz, R., Porins from bacterial and mitochondrial outer membranes. CRC Cr. Rev. Biochem.19 (1985) 145–190.
Benz, R., Structure and function of porins from gram-negative bacteria. A. Rev. Microbiol.42 (1988) 359–393.
Benz, R., Janko, K., Boos, W., and Läuger, P., Formation of large, ion-permeable membrane channels by the matrix protein (porin) ofEscherichia coli. Biochim. biophys. Acta511 (1978) 305–319.
Benz, R., Janko, K., and Läuger, P., Ionic selectivity of pores formed by the matrix protein (porin) ofEscherichia coli. Biochim. biophys. Acta551 (1979) 238–247.
Benz, R., Ludwig, O., De Pinto, V., and Palmieri, F., Permeability properties of mitochondrial porins of different eukaryotic cells, in: Achievements and Perspectives of Mitochondrial Research, vol. 1, pp. 317–327. Eds Quagliarello et al. Elsevier, Amsterdam 1985.
Benz, R., Wojtczak, L., Bosch, W., and Brdiczka, D., Inhibition of adenine nucleotide transport through the mitochondrial porin by a synthetic polyanion. FEBS Lett.210 (1988) 75–80.
Bessman, S. P., and Carpenter, C. L., The creatine creatine-phosphate energy shuttle. A. Rev. Cytochem.54, (1985) 831–865.
Brdiczka, D., Knoll, G., Riesinger, I., Weiler, U., Klug, G., Benz, R., and Krause, J., Microcompartmentation at the mitochondrial surface: its function in metabolic regulation, in: Myocardial and Skeletal Muscle Bioenergetics, pp. 55–69. Ed. N. Brautbar. Plenum Press, New York 1986.
Colombini, M., A candidate for the permeability pathway of the outer mitochondrial membrane. Nature279 (1979) 643–645.
Colombini, M., Pore size and properties of channels from mitochondria isolated fromNeurospora crassa, J. Membr. Biol.53 (980) 79–84.
Colombini, M., Holden, M.J., and Mangan, P., Modulation of the mitochondrial channel VDAC by a variety of agents, in: Anion Carriers of Mitochondrial Membranes, pp. 215–224. Eds A. Azzi et al. Springer, Heidelberg/New York 1989.
De Pinto, V., Ludwig, O., Krause, J., Benz, R., and Palmieri, F., Porin pores of mitochondrial outer membranes from high and low eukaryotic cells: biochemical and biophysical characterization. Biochim. biophys. Acta894 (1987) 109–119.
De Pinto, V., Prezioso, G., and Palmieri, F., A simple and rapid method for the purification of the mitochondrial porin from mammalian sources. Biochim. biophys. Acta905 (1987) 499–502.
Dihanich, M., Schmid, A., Oppliger, W., and Benz, R., Identification of a new pore in the mitochondrial outer membrane of a porin-deficient yeast mutant. Eur. J. Biochem.181 (1989) 703–708.
Fiek, C., Benz, R., Roos, N., and Brdiczka, D., Evidence for identity between the hexokinase-binding protein and the mitochondrial porin in the outer membrane of rat liver mitochondria. Biochim. biophys. Acta688 (1982) 429–440.
Freitag, H., Neupert, W., and Benz, R., Purification and characterization of a pore protein of the outer mitochondrial membrane fromNeurospora crassa. Eur. J. Biochem.123 (1982) 629–636.
Gellerich, F. N., Schlame, M., Bohnensack, R., and Kunz, W., Dynamic compartmentation of adenine nucleotides in the mitochondrial intermembrane space of rat-heart mitochondria. Biochim. biophys. Acta890 (1987) 117–126.
Kleene, R., Pfanner, N., Pfaller, R., Link, T.A., Sebald, W., Neupert, W., and Tropschug, M., Mitochondrial porin ofNeurospora crassa: cDNA cloning, in vitro expression and import into mitochondria. EMBO J.9 (1987) 2627–2633.
König, T., Kocsis, B., Meszarols, L., Nahm, K., Zoltan, S., and Horvath, I., Interaction of a synthetic polyanion with rat liver mitochondria. Biochim. biophys. Acta462 (1977) 380–389.
König, T., Stipani, I., Horvath, I., and Palmieri, F., Inhibition of mitochondrial substrate anion translocators by a synthetic amphipatic polyanion. J. Bioenerg. Biomembr.14 (1982) 297–305.
Lindén, M., Gellerfors, P., and Nelson, B. D., Purification of a protein having pore forming activity from the rat liver mitochondrial outer membrane. Biochem. J.208 (1982) 77–82.
Lindén, M., Gellerfors, P. and Nelson, B.D., Pore protein and hexokinase-binding protein from the outer membrane of rat liver mitochondria are identical. FEBS Lett.141 (1982) 189–192.
Ludwig, O., Benz, R., and Schultz, I. E., Porin ofParamecium mitochondria: Isolation, characterization and ion selectivity of the closed state. Biochim. biophys. Acta978 (1989) 319–327.
Ludwig, O., De Pinto, V., Palmieri, F., and Benz, R., Pore formation by the mitochondrial porin of rat brain mitochondria. Biochim. biophys. Acta860 (1986) 268–276.
Ludwig, O., Krause, J., Hay, R., and Benz, R., Purification and characterization of the pore forming protein of yeast mitochondrial outer membrane. Eur. Biophys. J.15 (1988) 269–276.
Mannella, C. A., and Frank, J., Negative staining characteristics of arrays of mitochondrial pore protein: Use of correspondence analysis to classify different staining patterns. Ultramicroscopy13 (1984) 93–102.
Mannella, C. A., and Frank, J., Electron microscopic stains as probes of the surface charge of mitochondrial outer membrane channels. Biophys. J.45 (1984) 139–141.
Michejda, J., Guo, X. J., and Lauquin, G. J.-M., Bioenergetic consequences of the lack of mitochondrial porin: Identification of a putative new pore, in: Anion Carriers of Mitochondrial Membranes, pp. 225–235. Eds A. Azzi et al. Springer, Heidelberg/New York 1989.
Mihara, K., and Sato, R., Molecular cloning and sequencing of cDNA of yeast porin, an outer mitochondrial membrane protein: a search for targeting signal in the primary structure. EMBO J.4 (1985) 769–774.
Ohlendieck, K., Riesinger, I., Adams, V., Krause, J., and Brdiczka, D., Enrichment and biochemical characterization of boundary membrane contact sites in rat-liver mitochondria. Biochim. biophys. Acta860 (1986) 672–689.
Roos, N., Benz, R. and Brdiczka, D., Identification and characterization of the pore-forming protein in the outer membrane of rat liver mitochondria. Biochim. biophys. Acta686 (1982) 204–214.
Schein, S. J., Colombini, M., and Finkelstein, A., Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained fromParamecium mitochondria. J. Membr. Biol.30 (1976) 99–120.
Wojtczak, L., and Zaluska, H., On the impermeability of the outer mitochondrial membrane to cytochrome c: I. Studies on whole mitochondria. Biochim. biophys. Acta193 (1969) 64–72.
Zalman, L. S., Nikaido, H., and Kagawa, Y., Mitochondrial outer membrane contains a protein producing nonspecific diffusion channels. J. biol. Chem.255 (1980) 1771–1774.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Benz, R. Biophysical properties of porin pores from mitochondrial outer membrane of eukaryotic cells. Experientia 46, 131–137 (1990). https://doi.org/10.1007/BF02027308
Published:
Issue Date:
DOI: https://doi.org/10.1007/BF02027308