Co-Authors:
Michal, O.-S., Department of Ornamental Horticulture, Agricultural Research Organization, The Volcani Center, P.O.B. 6, Bet Dagan, 50250, Israel
Sai, P.S.M., Departments of Biochemistry and Plant Genetics, Weizmann Institute of Science, Rehovot 76100 76100, Israel
Scherz, A., Departments of Biochemistry and Plant Genetics, Weizmann Institute of Science, Rehovot 76100 76100, Israel
Edelman, M., Departments of Biochemistry and Plant Genetics, Weizmann Institute of Science, Rehovot 76100 76100, Israel
Abstract:
A chlorophyll-protein complex has been isolated from the cyanobacterium Synechocystis sp. PCC 6803 that closely resembles higher plant photosystem II reaction centers in spectral properties. The Synechocystis complex has a pigment content of 5-7 chlorophyll a molecules: 1 Cyt 6559:2 pheophytins; an optical absorption redmost transition at ~675 nm; and a nonconservative circular dichroism red signal, with extrema at 682 (+) and 652 (-) nm. Upon illumination, the Synechocystis Dl/D2/Cyt 6559 complex accumulates reduced pheophytin. LDS-PAGE and/or immunoblotting showed the DI, D2, and Cyt 6559 proteins, aggregated and degraded forms of DI and possibly D2, and traces of ATP synthase and the CP47 photosystem II chlorophyll protein. The availability of such a Synechocystis preparation opens the way for employing site-directed mutagenesis in studying primary reactions of oxygenic photosynthesis. © 1995, American Chemical Society. All rights reserved.
תפריט נגישות
ניגודיות עדינה
מונוכרום
הדגשת קישורים
חסימת אנימציה
פונט קריא
סגור
איפוס הגדרות נגישות
להורדת מודול נגישות חינם
