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Autor:
Mazzullo, Mario, Bartoli, Silvana, Bonora, Bruna, Colacci, Annamaria, Grilli, Sandro, Lattanzi, Giovanna, Niero, Alessandra, Turina, Maria Paola, Parodi, Silvio
Publikováno v:
Environmental Health Perspectives, 1989 Jul 01. 82, 259-266.
Externí odkaz:
https://www.jstor.org/stable/3430784
We have recently shown that the H+/ATP ratio can significantly decrease during ATP hydrolysis by the ATPsynthase of Rb. capsulatus, when the concentration of either ADP or Pi is maintained at a low level. This same phenomenon has then been observed i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4094::97d1c7e51791a4e7b22659716dee1a50
http://hdl.handle.net/11585/123013
http://hdl.handle.net/11585/123013
La spiegazione della coscienza pone numerosi interrogativi sia di tipo scientifico che filosofico. Il testo è un contributo approfondito a questo tipo di ricerche, tentando di intrecciare apporti provenienti da varie discipline in un'analisi che aff
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4094::c24d955eeae0b957a0c7ae9341b7d04c
http://hdl.handle.net/11585/65109
http://hdl.handle.net/11585/65109
The H+/ATP ratio is an important parameter for energy balance in cells and for the mechanism of coupling between proton transport and ATP synthesis. Rotational catalysis predicts that the H+/ATP coincides with the ratio of the c-subunits to the β-su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4094::3c55940dcaf73f0c13ce020612e872aa
http://hdl.handle.net/11585/123020
http://hdl.handle.net/11585/123020
Autor:
Feniouk B. A., Anefors S., Mulkidjanian A. Y., Junge W., REBECCHI, ALBERTO, GIOVANNINI, DONATELLA, TURINA, MARIA PAOLA, MELANDRI, BRUNO ANDREA
H+-FOF1-ATP synthase couples proton flow through its membrane portion, FO, to the synthesis of ATP in its headpiece, F1. Upon reversal of the reaction the enzyme functions as a proton pumping ATPase. Even in the simplest bacterial enzyme the ATPase a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4094::2c8fc434244d8164c1c749f7a1a4d288
http://hdl.handle.net/11585/47713
http://hdl.handle.net/11585/47713
The H+/ATP ratio in the catalysis of ATP synthase has generally been considered a fixed parameter. However, in the ATP synthase of the photosynthetic bacterium Rhodobacter capsulatus, we have recently shown that this ratio can significantly decrease
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4094::c0def2ba17a19c9b653114d03c243f0f
http://hdl.handle.net/11585/123034
http://hdl.handle.net/11585/123034
The single-site mutation M23-K in the gamma-subunit of the E.coli ATP synthase has been reported to perturb the energetic coupling between F1 and FO and to increase the transition state activation energy for ATP hydrolysis (1). We have introduced the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4094::2a8beb3c557e6444a05bdd36f0b5231a
http://hdl.handle.net/11585/123036
http://hdl.handle.net/11585/123036
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4094::bea77d406185d0ec81b65e2e82c1fa60
http://hdl.handle.net/11585/1834
http://hdl.handle.net/11585/1834
In ATP synthases from several sources an uncoupling between ATP hydrolysis and proton pumping has been occasionally reported as a result of chemical modifications or mutagenesis.In the work to be presented, an intrinsic uncoupling has been found in t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______4094::d427b6bef73e2612581db1aa36cd2287
http://hdl.handle.net/11585/123043
http://hdl.handle.net/11585/123043