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Plant Physiology 57:577-579 (1976)
© 1976 American Society of Plant Biologists

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Articles

Evidence for a Block between Plastoquinone and Cytochrome f in a Photosynthetic Mutant of Lemna with Abnormal Flowering Behavior

Yosepha Shahak, Herbert B. Posner1 and Mordhay Avron

a Department of Biochemistry, Weizmann Institute of Science, Rehovot, Israel

Mutant strain 1073 of Lemna perpusilla is concluded to be blocked between plastoquinone and cytochrome f in the photosynthetic electron transport system. The location of the block is based on the following observations of activities in chloroplasts isolated from the mutant and wild-type plants. (a) Relative to wild type, electron flow rates from water to ferricyanide, 2,6-dichlorophenol indophenol or NADP were very low in the mutant, but rates of photosystem I-dependent electron flow and cyclic phosphorylation were high. (b) Chlorophyll a fluorescence induction curves for mutant and wild type were similar. (c) Silicomolybdate and lipophilic acceptors in the mutant were photoreduced at rates comparable to wild type. (d) Cytochrome f of the mutant chloroplasts was not reduced by red light, but was oxidized by red or far red light. (e) Reduction of the primary electron acceptor of photosystem II (Q) by ATP-driven reverse electron flow was not observed in the mutant.

1 On leave from Department of Biological Sciences, State University of New York at Binghamton, N. Y. 13901. Supported by a SUNY Research Foundation Faculty Research Fellowship.




This article has been cited by other articles:


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 Proc. Natl. Acad. Sci. USAHome page
A. V. Vener, P. J. M. van Kan, P. R. Rich, I. Ohad, and B. Andersson
Plastoquinol at the quinol oxidation site of reduced cytochrome bf mediates signal transduction between light and protein phosphorylation: Thylakoid protein kinase deactivation by a single-turnover flash
PNAS, February 18, 1997; 94(4): 1585 - 1590.
[Abstract] [Full Text] [PDF]

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 J. Biol. Chem.Home page
A. V. Vener, P. J. M. van Kan, A. Gal, B. Andersson, and I. Ohad
Activation/Deactivation Cycle of Redox-controlled Thylakoid Protein Phosphorylation
J. Biol. Chem., October 20, 1995; 270(42): 25225 - 25232.
[Abstract] [Full Text] [PDF]


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Copyright © 1976 by the American Society of Plant Biologists