TY - JOUR
T1 - Reversible optical control of F1Fo-ATP synthase using photoswitchable inhibitors
AU - Eisel, Bianca
AU - Hartrampf, Felix W.W.
AU - Meier, Thomas
AU - Trauner, Dirk
N1 - Funding Information:
We thank J?rgen Reichert (Max-Planck-Institute of Biophysics, Frankfurt am Main, Germany) who designed and constructed the device for the UV measurements (Fig.?S1). We also thank Werner K?hlbrandt for his support and lab space. This work was financially supported by the Deutsche Forschungsgemeinschaft (SFB 807 and SFB 1032) and the Wellcome Trust (WT110068/Z/15/Z).
Funding Information:
We thank Ju€rgen Reichert (Max-Planck-Institute of Biophysics, Frankfurt am Main, Germany) who designed and constructed the device for the UV measurements (Fig. S1). We also thank Werner Kühl-brandt for his support and lab space. This work was financially supported by the Deutsche Forschungsge-meinschaft (SFB 807 and SFB 1032) and the Wellcome Trust (WT110068/Z/15/Z).
Publisher Copyright:
© 2018 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies
PY - 2018/2
Y1 - 2018/2
N2 - F1Fo-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 lipolyticaATP synthase by light. Our experiments indicate that the PIAS bind to the same site in the ATP synthase F1 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.
AB - F1Fo-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 lipolyticaATP synthase by light. Our experiments indicate that the PIAS bind to the same site in the ATP synthase F1 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.
KW - Yarrowia lipolytica FF-ATP synthase
KW - photopharmacology
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U2 - 10.1002/1873-3468.12958
DO - 10.1002/1873-3468.12958
M3 - Article
C2 - 29292505
AN - SCOPUS:85041207914
VL - 592
SP - 343
EP - 355
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 3
ER -