Stabilization of chlorophyll a-binding apoproteins P700, CP47, CP43, D2, and D1 against proteolytic degradation has been investigated through in vitro synthesis of chlorophyll a or Zn-pheophytin a in intact etioplasts from barley. Stabilization of the apoproteins was dependent on the concentration of chlorophyll a or Znpheophytin a. Zn-pheophytin a was superior to chlorophyll a with respect to the concentration of pigment required for an equal yield of the stabilized chlorophyll a protein CP47, CP43, and P700 and for the total yield of chlorophyll a proteins. Zn-pheophytin a was most efficient for stabilizing CP47 and, at an increased concentration, efficient for stabilizing CP43, P700, and D1. Stabilization of apoproteins was highest after de novo synthesis of 90 -300 pmol of Zn-pheophytin a or of about 400 -600 pmol of chlorophyll a/4.2 ؋ 10 7 etioplasts. The yield of stabilized chlorophyll proteins decreased at higher concentrations of Zn-pheophytin a, but was unaffected by higher concentrations of chlorophyll a.The biogenesis of higher plant photosystems I and II requires assembly of nuclear-and plastid-encoded apoproteins with cofactors (e.g. chlorophyll, carotenoid, heme, quinone, iron, and manganese) within the inner plastid membrane system. Chlorophyll a (Chl) 1 is the key chromophore for higher plants to carry out the photosynthetic light reactions and is known to regulate the accumulation of the nuclear-and plastid-encoded apoproteins of the photosystems (1-4).Etioplasts isolated from 4-day-old, dark-grown barley are ideal to study the Chl-dependent accumulation of plastid-encoded photosystem proteins. Etioplasts in barley are formed from proplastids, during early primary leaf and plastid development, which proceeds uninhibited in the absence of light (5, 6).In the dark, etioplasts do not synthesize Chl and neither accumulate plastid-encoded Chl a-binding proteins (Chl aP) (7, 8) nor nuclear-encoded Chl a/b-binding apoproteins (1, 2), although they accumulate protochlorophyllide (Pchlide), a Chl precursor. When plants are illuminated, Pchlide is reduced to chlorophyllide (Chlide) in the plastid by protochlorophyllide oxidoreductase (9) in a light-and NADPH-dependent reaction. Illumination leads to disintegration of the prolamellar body and its dispersal into the primary lamellar layers of the prothylakoid membrane (10). Chlide is esterified with geranylgeranylpyrophosphate (GGPP) to yield Chl GG in a lightindependent enzymatic step catalyzed by chlorophyll synthase (11-13). In addition to the prenylation of the natural substrates Chlide a and b, chlorophyll synthase prenylates modified tetrapyrrol derivatives (14). Pentacoordinate metals (e.g. magnesium or zinc) are accepted as central atoms of the tetrapyrrole substrate, whereas metal-free pheophorbides or typical tetracoordinate central atoms (e.g. copper, nickel) do not act as a substrate for the enzyme (15). In isolated plastids Chl formation is accompanied by the accumulation of the plastid-encoded Chl-binding apoproteins (8) and assembly of the...