The water-exposed C-terminal sequence of bacteriorhodopsin does not affect H+ pumping
| Autor: | Vladimir P. Skulachev, L.A. Drachev, Yu.A. Ovchinnikov, A.V. Kiselev, Andrey D. Kaulen, N.G. Abdulaev |
|---|---|
| Rok vydání: | 1986 |
| Předmět: |
biology
Chemistry Sonication Kinetics Biophysics Bacteriorhodopsin Sequence (biology) Cell Biology biology.organism_classification Biochemistry Decomposition Crystallography Deprotonation Structural Biology Bacteriorhodopsin Kinetics Genetics biology.protein Halobacteriaceae H+ pumping Molecular Biology Photosystem |
| Zdroj: | FEBS Letters. 194:16-20 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(86)80043-6 |
| Popis: | The fast kinetics of photocycle and H+-pumping activity of papain-treated bacteriorhodopsin deprived of 17 C-terminal amino acid residues has been investigated. As demonstrated by a single-turnover study, the formation and decomposition of the M412 intermediate as well as the generation of the photoelectric potential are similar in the native and in the papain-treated protein. On the other hand, acidification of the medium caused by the deprotonation of bacteriorhodopsin due to M412 formation is much smaller in the C-tail-deprived protein. Short-term sonication or addition of a small amount of detergent completely abolishes this effect. As a result, papain-treated bacteriorhodopsin exhibits the same acidification as the native one. It is concluded that a decrease in the light-induced pH response of the C-tail-deprived bacteriorhodopsin is caused by the aggregation of purple sheets rather than by a special role of the C-terminal sequence in H+ pumping. |
| Databáze: | OpenAIRE |
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