2024-03-28T17:09:40Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/1808092020-04-15T10:51:19Zcom_10261_35com_10261_5col_10261_288
2019-04-30T12:21:48Z
urn:hdl:10261/180809
Fluorescence resonance energy transfer in single enzyme molecules with a quantum dot as donor
Gálvez Buerba, Eva Mª
Zimmermann, Boris
Rombach-Riegraf, Verena
Bienert, Roland
Gräber, P.
German Research Foundation
Gálvez Buerba, Eva Mª [0000-0001-6928-5516]
Single pair FRET
Fluorescence resonance energy transfer
Nanomotor
Quantum dots
H+-ATPsynthase
3 Figuras
H+-ATPsynthases couple a transmembrane proton transport with ATP synthesis and ATP hydrolysis. Previously, the relative subunit movement during this process has been measured by fluorescence resonance energy transfer (FRET) between two organic fluorophores covalently bound to different subunits. To improve the photophysical stability, a luminescent CdSe/ZnS nanocrystal (quantum dot) was bound to the enzyme and an organic fluorophore, Alexa568, was used as fluorescence acceptor. Single-molecule spectroscopy with the membrane integrated labeled H+-ATPsynthase was carried out. Single-pair FRET indicates three different conformations of the enzyme. During ATP hydrolysis relative intramolecular subunit movements are observed in real time.
2019-04-30T12:21:48Z
2019-04-30T12:21:48Z
2008-06-27
artículo
European Biophysics Journal 37: 1367-1371 (2008)
0175-7571
http://hdl.handle.net/10261/180809
10.1007/s00249-008-0351-7
1432-1017
http://dx.doi.org/10.13039/501100001659
eng
http://dx.doi.org/10.1007/s00249-008-0351-7
Sí
closedAccess
Springer