Effects of high temperatures on the photosynthetic systems in spinach: Oxygen-evolving activities, fluorescence characteristics and the denaturation process

Activities of oxygen evolution, fluorescence F-v (a variable part of chlorophyll fluorescence) values, and amounts of the 33 kDa protein remaining bound to the thylakoids in intact spinach chloroplasts were measured during and after high-temperature treatment. The following results were obtained. (1) Both the F-v value and the flash-induced oxygen evolution measured by an oxygen electrode were decreased at high temperatures, but they showed partial recovery when the samples were cooled down and incubated at 25 degrees C for 5 min after high-temperature treatment. (2) Oxygen evolution was more sensitive to high temperatures than the F-v value, and the decrease in the F-v/F-m ratio at high temperatures rather corresponded to that in the oxygen evolution measured at 25 degrees C after high-temperature treatment. (3) Photoinactivation of PS II was very rapid at high temperatures, and this seems to be a cause of the difference between the F-v values and the oxygen-evolving activities at high temperatures. (4) At around 40 degrees C, the manganese-stabilizing 33 kDa protein of PS II was supposed to be released from the PS II core complexes during heat treatment and to rebind to the complexes when the samples were cooled down to 25 degrees C. (5) At higher temperatures, the charge separation reaction of PS II was inactivated, and the PS II complexes became less fluorescent, which was recovered partially at 25 degrees C. (6) Increases in the F-v value due to a large decrease in the electron flow from Q(A) to Q(B) became prominent after high-temperature treatment at around 50 degrees C. This was the main cause of the discrepancy between the F-v values and the oxygen-evolving activities measured at 25 degrees C. Relationship between the process of heat inactivation of PS II reaction center complexes and the fluorescence levels is discussed.