The 33 kDa protein of photosystem II is a low-affinity calcium-and lanthanide-binding protein
J Kruk, K Burda, M Jemioła-Rzemińska, K Strzałka - Biochemistry, 2003 - ACS Publications
J Kruk, K Burda, M Jemioła-Rzemińska, K Strzałka
Biochemistry, 2003•ACS PublicationsWe have shown that the isolated 33 kDa protein of photosystem II contains one calcium and
one lanthanide low-affinity binding site with binding constants (KD) on the order of 10-5 M.
Binding of calcium or lanthanides to this site induces conformational changes in the protein
that manifest in fluorescence emission spectra of the protein, circular dichroism spectra, and
calorimetric thermograms where the phase transitions are shifted to lower temperatures. The
role of calcium binding to the 33 kDa protein in the attainment of its native structure and the …
one lanthanide low-affinity binding site with binding constants (KD) on the order of 10-5 M.
Binding of calcium or lanthanides to this site induces conformational changes in the protein
that manifest in fluorescence emission spectra of the protein, circular dichroism spectra, and
calorimetric thermograms where the phase transitions are shifted to lower temperatures. The
role of calcium binding to the 33 kDa protein in the attainment of its native structure and the …
We have shown that the isolated 33 kDa protein of photosystem II contains one calcium and one lanthanide low-affinity binding site with binding constants (KD) on the order of 10-5 M. Binding of calcium or lanthanides to this site induces conformational changes in the protein that manifest in fluorescence emission spectra of the protein, circular dichroism spectra, and calorimetric thermograms where the phase transitions are shifted to lower temperatures. The role of calcium binding to the 33 kDa protein in the attainment of its native structure and the significance of this interaction for the oxygen evolution process are discussed.
ACS Publications