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231223s2009 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/erp242
|2 doi
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|a pubmed24n0635.xml
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|a (DE-627)NLM190510684
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|a (NLM)19661266
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Eichelmann, H
|e verfasserin
|4 aut
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|a Rubisco in planta kcat is regulated in balance with photosynthetic electron transport
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|c 2009
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 01.02.2010
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|a Date Revised 20.10.2021
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Site turnover rate (k(cat)) of Rubisco was measured in intact leaves of different plants. Potato (Solanum tuberosum L.) and birch (Betula pendula Roth.) leaves were taken from field-growing plants. Sunflower (Helianthus annuus L.), wild type (wt), Rubisco-deficient (-RBC), FNR-deficient (-FNR), and Cyt b(6)f deficient (-CBF) transgenic tobacco (Nicotiana tabacum L.) were grown in a growth chamber. Rubisco protein was measured with quantitative SDS-PAGE and FNR protein content with quantitative immunoblotting. The Cyt b(6)f level was measured in planta by maximum electron transport rate and the photosystem I (PSI) content was assessed by titration with far-red light. The CO(2) response of Rubisco was measured in planta with a fast-response gas exchange system at maximum ribulose 1,5-bisphosphate concentration. Reaction site k(cat) was calculated from V(m) and Rubisco content. Biological variation of k(cat) was significant, ranging from 1.5 to 4 s(-1) in wt, but was >6 s(-1) at 23 degrees C in -RBC leaves. The lowest k(cat) of 0.5 s(-1) was measured in -FNR and -CBF plants containing sufficient Rubisco but having slow electron transport rates. Plotting k(cat) against PSI per Rubisco site resulted in a hyperbolic relationship where wt plants are on the initial slope. A model is suggested in which Rubisco Activase is converted into an active ATP-form on thylakoid membranes with the help of a factor related to electron transport. The activation of Rubisco is accompanied by the conversion of the ATP-form into an inactive ADP-form. The ATP and ADP forms of Activase shuttle between thylakoid membranes and stromally-located Rubisco. In normal wt plants the electron transport-related activation of Activase is rate-limiting, maintaining 50-70% Rubisco sites in the inactive state
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Plant Proteins
|2 NLM
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|a Ribulose-Bisphosphate Carboxylase
|2 NLM
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| 650 |
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|a EC 4.1.1.39
|2 NLM
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|a Talts, E
|e verfasserin
|4 aut
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|a Oja, V
|e verfasserin
|4 aut
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|a Padu, E
|e verfasserin
|4 aut
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| 700 |
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|a Laisk, A
|e verfasserin
|4 aut
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 60(2009), 14 vom: 15., Seite 4077-88
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
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|g volume:60
|g year:2009
|g number:14
|g day:15
|g pages:4077-88
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|u http://dx.doi.org/10.1093/jxb/erp242
|3 Volltext
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|d 60
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|e 14
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|h 4077-88
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