Autor: |
TURINA, MARIA PAOLA, GIOVANNINI, DONATELLA, GUBELLINI, FRANCESCA, MELANDRI, BRUNO ANDREA |
Přispěvatelé: |
TURINA M.P., GIOVANNINI D., GUBELLINI F., MELANDRI B. |
Jazyk: |
angličtina |
Rok vydání: |
2004 |
Předmět: |
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Popis: |
The proton-pumping and the ATP hydrolysis activities of the ATP synthase of Rhodobacter capsulatus have been compared as a function of the ADP and Pi concentrations. The proton pumping was measured either with the transmembrane pH difference probe, 9-amino-6-chloro-2-methoxyacridine, or with the transmembrane electric potential difference probe, bis(3-propyl-5-oxoisoxazol-4-yl)pentamethine oxonol, obtaining consistent results. The comparison indicates that an intrinsic uncoupling of ATP synthase is induced when the concentration of either ligand is decreased. The half-maximal effect was found in the submicromolar range for ADP and at about 70 M for Pi. It is proposed that a switch from a partially uncoupled state of ATP synthase to the coupled state is induced by the simultaneous binding of ADP and Pi. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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