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The ATP synthase in chromatophores of Rhodobacter caspulatus can effectively generate a transmembrane pH difference coupled to the hydrolysis of ATP. The rate of hydrolysis was rather insensitive to the depletion of ADP in the assay medium by an ATP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::452a7d8d8239300cd1f027b35293af86
http://hdl.handle.net/11585/33110
http://hdl.handle.net/11585/33110
Autor:
Wolfgang Junge, Armen Y. Mulkidjanian, Sofie Anefors, Paola Turina, Boris A. Feniouk, Alberto Rebecchi, B. Andrea Melandri, Donatella Giovannini
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. (11):1319-1330
H(+)-F(O)F(1)-ATP synthase couples proton flow through its membrane portion, F(O), to the synthesis of ATP in its headpiece, F(1). Upon reversal of the reaction the enzyme functions as a proton pumping ATPase. Even in the simplest bacterial enzyme th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3c861ffe8b9577067b5a649c5714dce
