Biosynthesis of P700-Chlorophyll a Protein Complex, Plastocyanin, and Cytochrome b(6)/f Complex.
نویسندگان
چکیده
Changes in the amount of P700-chlorophyll a protein complex, plastocyanin, and cytochrome b(6)/f complex during greening of pea (Pisum sativum L.), wheat (Triticum aestivum L.), and barley (Hordeum vulgare L.) leaves were analyzed by an immunochemical quantification method. Neither subunit I nor II of P700-chlorophyll a protein complex could be detected in the etiolated seedlings of all three plants and the accumulation of these subunits was shown to be light dependent. On the other hand, a small amount of plastocyanin was present in the etiolated seedlings of all three plants and its level increased about 30-fold during the subsequent 72-hour greening period. Furthermore, cytochrome f, cytochrome b(6), and Rieske Fe-S center protein in cytochrome b(6)/f complex were also present in the etiolated seedings of all three plants. The level of each subunit component increased differently during greening and their induction pattern differed from species to species. The accumulation of cytochrome b(6)/f complex was most profoundly affected by light in pea leaves, and the levels of cytochrome f, cytochrome b(6), and Rieske Fe-S center protein increased during greening about 10-, 20-, and more than 30-fold, respectively. In comparison to the case of pea seedlings, in wheat and barley leaves the level of each subunit component increased much less markedly. The results suggest that light regulates the accumulation of not only the chlorophyll protein complex but also the components of the electron transport systems.
منابع مشابه
Photooxidation of Cytochromes c, f, and Plastocyanin by Detergent Treated Chloroplasts.
Nieman et al. (16,17) and Bishop et al. (2) described the photooxidation of ferrocytochrome c by detergent treated chloroplasts as an oxygen-consuming, cyanide-insensitive process which was stimulated by a soluble chloroplast enzyme. In an earlier paper, we reported that the quantum yield of this reaction increases at wavelengths beyond 690 my (14), and concluded that only the first photoact is...
متن کاملDefects in the cytochrome b6/f complex prevent light-induced expression of nuclear genes involved in chlorophyll biosynthesis.
Mutants with defects in the cytochrome (cyt) b6/f complex were analyzed for their effect on the expression of a subgroup of nuclear genes encoding plastid-localized enzymes participating in chlorophyll biosynthesis. Their defects ranged from complete loss of the cytb6/f complex to point mutations affecting specifically the quinone-binding QO site. In these seven mutants, light induction of the ...
متن کاملEffect of trypsin treatment of photosystem I particles on the electron donation to p700.
Proteolysis of photosystem I particles had no effect on P700 oxidation but did inhibit the rate of P700(+) reduction. The V(max) values were decreased for both dichlorophenol and plastocyanin, but the K(m) values were unaffected indicating that trypsin treatment altered electron transfer rather than the binding of the donor to the photosystem I complex. The salt dependence of P700(+) reduction ...
متن کاملThe photochemical activities and electron carriers of developing barley leaves.
The development of photochemical activities in isolated barley plastids during illumination of dark-grown plants has been studied and compared with the behaviour of plastocyanin, cytochromes f, b-559(LP), b-563 and b-559(HP) and pigments P546 (C550) and P700. Electron-transport activity dependent on Photosystem 1 and cyclic photophosphorylation dependent on N-methylphenazonium methosulphate (ph...
متن کاملEquilibration between cytochrome f and P700 in intact leaves.
Electron transport between the two photosynthetic reaction centres of high plants is mediated by plastoquinone, a rieske iron-sulfur centre, cytochrome f and plastocyanin. Measurements of redox equilibration amongst these have produced confusing results, with apparent equilibrium constants being estimated that are inconsistent with in vitro measurements of redox midpoint potentials of the compo...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Plant physiology
دوره 81 1 شماره
صفحات -
تاریخ انتشار 1986