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Reversible optical control of F 1 F o ‐ ATP synthase using photoswitchable inhibitors
Author(s) -
Eisel Bianca,
Hartrampf Felix W.W.,
Meier Thomas,
Trauner Dirk
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12958
Subject(s) - atp synthase , biochemistry , yarrowia , enzyme , chemistry , atp synthase gamma subunit , fatty acid synthase , yeast , atpase , atp hydrolysis
F 1 F o ‐ ATP synthase is one of the best studied macromolecular machines in nature. It can be inhibited by a range of small molecules, which include the polyphenols, resveratrol and piceatannol. Here, we introduce Photoswitchable Inhibitors of ATP Synthase, termed PIAS , which were synthetically derived from these polyphenols. They can be used to reversibly control the enzymatic activity of purified yeast Yarrowia lipolytica ATP synthase by light. Our experiments indicate that the PIAS bind to the same site in the ATP synthase F 1 complex as the polyphenols in their trans form, but they do not bind in their cis form. The PIAS could be useful tools for the optical precision control of ATP synthase in a variety of biochemical and biotechnological applications.