Stabilization of the chlorophyll binding apoproteins, P700, CP47, CP43, D2, and D1, by synthesis of Zn-pheophytin a in intact etioplasts from barley.
Chlorophyll a was compared with Zn-pheophytin a for stabilization of chlorophyll binding apoproteins, P700, CP47, CP43, D2, and D1, in intact etioplasts from barley (Hordeum vulgare L.). Intact etioplasts were shown to effectively translate the chlorophyll apoproteins, to take up and esterify the exogenously added substrates, chlorophyllide a and Zn-pheophorbide a, with geranylgeraniolpyrophosphate. For stabilization of P700, CP47, D2, and D1, the product, Zn-pheophytin a, was shown to substitute for chlorophyll a. Stabilization of CP43 was selectively increased in the presence of Zn-pheophytin a. The degree of stabilization was shown to depend on the amount of newly synthesized Zn-pheophytin a and on the central atom of the chlorophyll molecule.
Department of Botany, University of Munich, Germany. Lutz@botanik.biologie.uni-muenchen.de
L A
LA
Eichacker
B
B
Müller
M
M
Helfrich
D002734:Chlorophyll / Q000378:metabolism*; D000077194:Chlorophyll A; D002736:Chloroplasts / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D001467:Hordeum / Q000378:metabolism*; D007700:Kinetics; D045342:Light-Harvesting Protein Complexes; D015388:Organelles / Q000378:metabolism; D045322:Photosynthetic Reaction Center Complex Proteins / Q000096:biosynthesis / Q000378:metabolism*; D045332:Photosystem II Protein Complex
D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; C083100:photosystem II, chlorophyll binding protein, CP-43; C070970:photosystem II, chlorophyll-binding protein, CP-47; D002734:Chlorophyll; D000077194:Chlorophyll A