Response of NAD(P)H dehydrogenase complex to the alteration of CO2 concentration in the cyanobacterium Synechocystis PCC6803

An NADPH-specific NDH-1 sub-complex was separated by native-polyacrylamide gel electrophoresis and detected by activity staining from the whole cell extracts of Synechocystis PCC6803. Low CO2 caused an increase in the activity of this sub-complex quickly, accompanied by an evident increase in the ex...

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Bibliographic Details
Published in:Journal of plant physiology 2003-08, Vol.160 (8), p.967-970
Main Authors: Deng, Y, Ye, J, Mi, H, Shen, Y
Format: Article
Language:English
Subjects:
bacterial proteins
Bacteriology
Biological and medical sciences
carbon dioxide
Carbon Dioxide - metabolism
Cyanobacteria - enzymology
Cyanobacteria - metabolism
Fundamental and applied biological sciences. Psychology
Kinetics
Metabolism. Enzymes
Microbiology
NADH dehydrogenase
NADH, NADPH Oxidoreductases - isolation & purification
NADH, NADPH Oxidoreductases - metabolism
NADP (coenzyme)
oxidation
photosystem I
plant proteins
signal transduction
Synechocystis sp. PCC 6803
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Summary:An NADPH-specific NDH-1 sub-complex was separated by native-polyacrylamide gel electrophoresis and detected by activity staining from the whole cell extracts of Synechocystis PCC6803. Low CO2 caused an increase in the activity of this sub-complex quickly, accompanied by an evident increase in the expression of NdhK and PSI-driven NADPH oxidation activity that can reflect the activity of NDH-1-mediated cyclic electron transport. During incubation with high CO2, the activities of NDH-1 sub-complex and PSI-driven NADPH oxidation as well as the protein level of NdhK slightly increased at the beginning, but decreased evidently in various degrees along with incubation time. These results suggest that CO2 concentration in vitro as a signal can control the activity of NDH-1 complex, and NDH-1 complex may in turn function in the regulation of CO2 uptake.
ISSN:0176-1617
1618-1328
DOI:10.1078/0176-1617-01053