TY - JOUR
T1 - A Light‐Triggered Adenosine Triphosphate‐Phosphate Exchange Reaction in Chloroplasts
AU - Carmeli, C.
AU - Avron, M.
PY - 1967/10
Y1 - 1967/10
N2 - Chloroplasts were triggered by light in the presence of dithiol reagents to catalyze an ATP‐Pi exchange reaction in a following dark period. This light‐triggered ATP‐Pi exchange was related to photophosphorylation, and to light‐triggered ATPase by the similarity in requirements for magnesium ions, phenazine methosulfate and flavin mononucleotide, and the inhibition by uncouplers and electron transport inhibitors. The ATP‐Pi exchange reaction showed substrate specificity for ATP and was competitively inhibited by ADP. The light‐triggered condition decayed in the dark with a half‐life of several minutes. The rate of the decay was not affected by uncouplers or energy transfer inhibitors. The light‐triggering phase required the presence of a dithiol‐reagent, and was stimulated by magnesium and electron transfer catalysts. The dark phase did not require the presence of dithiol reagents. The energy transfer inhibitors DIO‐9 and phloridzin as well as the uncoupler atebrin and the inhibitor n‐butyl‐3,5‐diiodo‐4‐hydroxybenzoate inhibited only the dark phase. The uncoupler, NH4CI, and the inhibitor 4,5,6,7‐tetrabromo‐2‐trifluoromethylbenzinamidazol inhibited both the light‐triggering phase and the dark phase. The overall pH optimum for ATP‐Pi exchange was about 8. However, the pH optimum of the light stage alone was about 9 and that of the dark stage — about 7.5. Chloroplast fragments which retain their capacity for photophosphorylation possessed light‐triggered ATP‐Pi exchange activity but had no light‐triggered ADP‐ATP exchange.
AB - Chloroplasts were triggered by light in the presence of dithiol reagents to catalyze an ATP‐Pi exchange reaction in a following dark period. This light‐triggered ATP‐Pi exchange was related to photophosphorylation, and to light‐triggered ATPase by the similarity in requirements for magnesium ions, phenazine methosulfate and flavin mononucleotide, and the inhibition by uncouplers and electron transport inhibitors. The ATP‐Pi exchange reaction showed substrate specificity for ATP and was competitively inhibited by ADP. The light‐triggered condition decayed in the dark with a half‐life of several minutes. The rate of the decay was not affected by uncouplers or energy transfer inhibitors. The light‐triggering phase required the presence of a dithiol‐reagent, and was stimulated by magnesium and electron transfer catalysts. The dark phase did not require the presence of dithiol reagents. The energy transfer inhibitors DIO‐9 and phloridzin as well as the uncoupler atebrin and the inhibitor n‐butyl‐3,5‐diiodo‐4‐hydroxybenzoate inhibited only the dark phase. The uncoupler, NH4CI, and the inhibitor 4,5,6,7‐tetrabromo‐2‐trifluoromethylbenzinamidazol inhibited both the light‐triggering phase and the dark phase. The overall pH optimum for ATP‐Pi exchange was about 8. However, the pH optimum of the light stage alone was about 9 and that of the dark stage — about 7.5. Chloroplast fragments which retain their capacity for photophosphorylation possessed light‐triggered ATP‐Pi exchange activity but had no light‐triggered ADP‐ATP exchange.
UR - http://www.scopus.com/inward/record.url?scp=0014143360&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1967.tb00141.x
DO - 10.1111/j.1432-1033.1967.tb00141.x
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AN - SCOPUS:0014143360
SN - 0014-2956
VL - 2
SP - 318
EP - 326
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 3
ER -