Summary
Limited proteolysis with proteases of different specificity has been used to obtain a number of preparations of the reaction center (RC) from the thermophilic green bacterium Chloroflexus aurantiacus. The absorption spectrum of the native RC are preserved in these preparations, even after the shortening of the N-termini of both RC subunits to different extent. Considerable part of the hydrophilic N-terminus of the L-subunit has been shown to be unaccessible to the proteases. AlaL3-ArgL25 region contribute to the thermal stability of the Chloroflexus RC.
Keywords
- Purple Bacterium
- Limited Proteolysis
- Phototrophic Bacterium
- Photosynthetic Reaction Center
- Primary Charge Separation
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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Kutuzov, M.A., Levina, N.B., Abdulaev, N.G., Zolotarev, A.S. (1990). Limited Proteolysis and Its Influence on Thermal Stability of the Photosynthetic Reaction Center from Chloroflexus aurantiacus . In: Drews, G., Dawes, E.A. (eds) Molecular Biology of Membrane-Bound Complexes in Phototrophic Bacteria. FEMS Symposium. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-0893-6_35
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DOI: https://doi.org/10.1007/978-1-4757-0893-6_35
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