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Plant Physiology 67:17-20 (1981)
© 1981 American Society of Plant Biologists

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Articles

Fluorescence Properties of Guard Cell Chloroplasts

EVIDENCE FOR LINEAR ELECTRON TRANSPORT AND LIGHT-HARVESTING PIGMENTS OF PHOTOSYSTEMS I AND II 1

Eduardo Zeiger2,3, Paul Armond4,5 and Anastasios Melis4

2 Department of Biological Sciences, Stanford University, Stanford, California 94305, 4 Department of Plant Biology, Carnegie Institution of Washington, Stanford, California 94305

The presence of chloroplasts in guard cells from leaf epidermis, coleoptile, flowers, and albino portions of variegated leaves was established by incident fluorescence microscopy, thus confirming the notion that guard cell chloroplasts are remarkably conserved. Room temperature emission spectra from a few chloroplasts in a single guard cell of Vicia faba showed one major peak at around 683 nanometers. Low-temperature (77 K) emission spectra from peels of albino portions of Chlorophytum comosum leaves and from mesophyll chloroplasts of green parts of the same leaves showed major peaks at around 687 and 733 nanometers, peaks usually attributed to photosystem II and photosystem I pigment systems, respectively. Spectra of peels of V. faba leaves showed similar peaks. However, fluorescence microscopy revealed that the Vicia peels, as well as those from Allium cepa and Tulipa sp., were contaminated with non-guard cell chloroplasts which were practically undetectable under bright field illumination. These observations pose restrictions on the use of epidermal peels as a source of isolated guard cell chloroplasts. Studies on the 3-(3,4-dichlorophenyl)-1,1-dimethylurea-sensitive variable fluorescence kinetics of uncontaminated epidermal peels of C. comosum indicated that guard cell chloroplasts operate a normal, photosystem II-dependent, linear electron transport. The above properties in combination with their reported inability to fix CO2 photosynthetically may render the guard cell chloroplasts optimally suited to supply the reducing and high-energy phosphate equivalents needed to sustain active ion transport during stomatal opening in daylight.


3 To whom reprint requests should be addressed.

5 Present address: Pfizer Central Research, Eastern Point Road, Groton, Connecticut 06340.

1 Research was supported by National Science Foundatio Grant PCM 77-17642 (to E. Z.) and a grant from the Andrew Mellon Foundation (to A. M.). This is Carnegie Institution of Washington-Department of Plant Biology publication No. 710.




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