Photosystem (PS) II particles prepared from spinach thylakoids with Triton X-100 were treated with 1.5 M NaCl either in the light or dark. Under both conditions, the 24-kDa and 18-kDa proteins were released from the particles, but rebound to them when the NaCl concentration was reduced to 34 mM by dilution. Oxygen evolution measured after the dilution was inactivated following NaCl treatment in the light, but not following treatment in the dark. The inactivation in the light was suppressed when 5 mM CaCl2 was added during or after the NaCl treatment. Based on these observations, a scheme is proposed for the mechanism of light-dependent inactivation of oxygen evolution during NaCl treatment of PS II particles and for the function of the 24-kDa protein in regulating the conformation of a supposed Ca2+-binding intrinsic protein.
|Number of pages||8|
|Publication status||Published - 1986 Jan 1|
ASJC Scopus subject areas
- Plant Science