Skip Navigation


Plant and Cell Physiology Advance Access originally published online on September 16, 2006
Plant and Cell Physiology 2006 47(10):1432-1436; doi:10.1093/pcp/pcl008
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
47/10/1432    most recent
pcl008v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (3)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Ma, W.
Right arrow Articles by Mi, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ma, W.
Right arrow Articles by Mi, H.
Agricola
Right arrow Articles by Ma, W.
Right arrow Articles by Mi, H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2006. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Short Communication

Active NDH-1 Complexes from the Cyanobacterium Synechocystis sp. Strain PCC 6803

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

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, PR China

* Corresponding author: E-mail, mihl{at}sippe.ac.cn; Fax, +86-21-54924015.

We identified eight bands by staining native gels for NADPH-nitroblue tetrazolium oxidoreductase activity after electrophoresis of n-dodecyl-ß-D-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 supercomplex of NDH-1 (about 1,000 kDa) that was absent in the {Delta}ndhD1/D2 mutant and was suppressed under low CO2. Band C was induced under low CO2 or in the {Delta}ndhD1/D2 mutant and was converted to bands D and E. Bands A and C appear to be an NDH-1L dimer and NDH-1M, respectively, with subunits essential for the activity.

(Received July 27, 2006; Accepted September 11, 2006)
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Plant Cell PhysiolHome page
M. Xu, T. Ogawa, H. B. Pakrasi, and H. Mi
Identification and Localization of the CupB Protein Involved in Constitutive CO2 Uptake in the Cyanobacterium, Synechocystis sp. Strain PCC 6803
Plant Cell Physiol., June 1, 2008; 49(6): 994 - 997.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.