Initial NMR and other spectroscopic studies of PsbO protein from Photosystem II
Sprache des Vortragstitels:
Englisch
Original Tagungtitel:
BISSL (Bilateral Impromptu Symposium (Stockholm-Linz) on NMR Spectroscopy
Sprache des Tagungstitel:
Englisch
Original Kurzfassung:
PsbO, also called 33 kDa thylakoid protein, is the biggest extrinsic protein of PS II
located on lumenal surface of this photosynthetic apparatus. Currently a Cryo-EM
structure with resolution of 3.2 Å from spinach including PsbO is available. The
protein with actual molecular weight 26 kDa has a characteristic ?-barrel structure
and high content of random coils similar to its cyanobacterial homologue. By in-
teracting with other two smaller extrinsic proteins, namely PsbP and PsbQ, the
heterotrimeric triangular PsbO?PsbP?PsbQ complex is formed and it serves to op-
timize the efficiency of oxygen evolution in PSII under physiological conditions.
Content of secondary structure of PsbO was estimated by CD and FTIR and state
of the sample prior to NMR measurements was controlled by Raman and fluo-
rescence spectroscopy. Currently PsbO has been subjected to NMR experiments
yielding incomplete information. In order to overcome line-broadening effect in
NMR experiments, expression of deuterated sample was tested. Amino acid selec-
tive unlabeling yielded valuable information for identification of peaks and future
assignment of PsbO.
Forschungs-