Energy transduction and transport processes in thermophilic bacteria
Autor: | Wn Konings, Arnold J. M. Driessen, M. G. L. Elferink, B. Tolner, J.G. de Wit, G Speelmans |
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Rok vydání: | 1992 |
Předmět: |
Physiology
Microbial metabolism Cell membrane medicine REACTION CENTERS TETRAETHER LIPIDS THERMOPHILES Integral membrane protein Thermostability CLOSTRIDIUM-FERVIDUS ENERGY TRANSDUCTION Bacteria biology SULFOLOBUS-ACIDOCALDARIUS MEMBRANE FUSION Thermophile ARCHAEBACTERIAE CYTOCHROME-C OXIDASE Temperature Biological Transport Cell Biology biology.organism_classification Archaea STREPTOCOCCUS-CREMORIS SOLUTE TRANSPORT EXTREMOPHILES RECONSTITUTION Membrane medicine.anatomical_structure Energy Transfer Membrane protein Biochemistry ESCHERICHIA-COLI AMINO-ACID-TRANSPORT BACILLUS-STEAROTHERMOPHILUS CHLOROFLEXUS-AURANTIACUS MEMBRANE-VESICLES |
Zdroj: | Journal of Bioenergetics and Biomembranes. 24:601-609 |
ISSN: | 1573-6881 0145-479X |
DOI: | 10.1007/bf00762352 |
Popis: | Bacterial growth at the extremes of temperature has remained a fascinating aspect in the study of membrane function and structure. The stability of the integral membrane proteins of thermophiles make them particularly amenable to study. Respiratory enzymes of thermophiles appear to be functionally similar to the mesophilic enzymes but differ in their thermostability and unusual high turnover rates. Energy coupling at extreme temperatures seems inefficient as suggested by the high maintenance coefficients and the high permeability of the cell membrane to protons. Nevertheless, membranes maintain their structure at these extremes through changes in fatty acid acyl chain composition. Archaebacteria synthesize novel membrane-spanning lipids with unique physical characteristics. Thermophiles have adapted to life at extreme temperatures by using sodium ions rather than protons as coupling ions in solute transport. Genetic and biochemical studies of these systems now reveal fundamental principles of such adaptations. The recent development of reconstitution techniques using membrane-spanning lipids allows a rigorous biochemical characterization of membrane proteins of extreme thermophiles in their natural environment. |
Databáze: | OpenAIRE |
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