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Plant and Cell Physiology Advance Access published online on September 16, 2006
Plant and Cell Physiology, doi:10.1093/pcp/pcl008
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© The Author 2006. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

Short Communication

Active NDH-1 complexes from the cyanobacterium Synechocystis sp. strain PCC 6803

Weimin Ma 1, Young Deng 1, Teruo Ogawa 1, and Hualing Mi 1 *

1 National Laboratory of Plant Molecular Genetics, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Graduate School of the Chinese Academy of Sciences, 300 Fenglin Road, Shanghai, 200032, China

* To whom correspondence should be addressed.
Hualing Mi, E-mail: mihl{at}sippe.ac.cn


  Abstract

We identified eight bands by staining the native gels for NADPH-nitroblue tetrazolium oxidoreductase activity after electrophoresis of n-dodecyl-ß-maltoside-treated membranes of Synechocystis sp. strain PCC 6803. Among them, bands A, C, D and E were attributed to the activity of NADPH dehydrogenase (NDH-1). Band A is a highly active super-complex of NDH-1 (about 1,000 kDa) that was absent in {Delta}ndhD1/D2 mutant and was suppressed under low CO2. Band C was induced under low CO2 or in {Delta}ndhD1/D2 mutant and was converted to bands D and E. Bands A and C appear to be NDH-1L dimer and NDH-1M, respectively, with subunits essential for the activity.

Keywords: Active NDH-1 complexes; activity staining; Synechocystis sp. strain PCC 6803.
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