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231224s2017 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/erx110
|2 doi
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|a pubmed24n0906.xml
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|a DE-627
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|a eng
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|a Raven, John A
|e verfasserin
|4 aut
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|a The possible evolution and future of CO2-concentrating mechanisms
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|c 2017
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 14.05.2018
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|a Date Revised 18.03.2022
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|a published: Print
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|a Citation Status MEDLINE
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|a © The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissionsoup.com.
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|a CO2-concentrating mechanisms (CCMs), based either on active transport of inorganic carbon (biophysical CCMs) or on biochemistry involving supplementary carbon fixation into C4 acids (C4 and CAM), play a major role in global primary productivity. However, the ubiquitous CO2-fixing enzyme in autotrophs, Rubisco, evolved at a time when atmospheric CO2 levels were very much higher than today and O2 was very low and, as CO2 and O2 approached (by no means monotonically), today's levels, at some time subsequently many organisms evolved a CCM that increased the supply of CO2 and decreased Rubisco oxygenase activity. Given that CO2 levels and other environmental factors have altered considerably between when autotrophs evolved and the present day, and are predicted to continue to change into the future, we here examine the drivers for, and possible timing of, evolution of CCMs. CCMs probably evolved when CO2 fell to 2-16 times the present atmospheric level, depending on Rubisco kinetics. We also assess the effects of other key environmental factors such as temperature and nutrient levels on CCM activity and examine the evidence for evolutionary changes in CCM activity and related cellular processes as well as limitations on continuity of CCMs through environmental variations
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|a Journal Article
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|a Review
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|a Research Support, Non-U.S. Gov't
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|a Algae
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|a CO2 diffusion
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|a CO2-concentrating mechanisms
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|a Rubisco
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|a cyanobacteria
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|a evolution
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|a Algal Proteins
|2 NLM
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|a Bacterial Proteins
|2 NLM
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|a Plant Proteins
|2 NLM
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|a Carbon Dioxide
|2 NLM
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|a 142M471B3J
|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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| 700 |
1 |
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|a Beardall, John
|e verfasserin
|4 aut
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|a Sánchez-Baracaldo, Patricia
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 68(2017), 14 vom: 01. Juni, Seite 3701-3716
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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|g volume:68
|g year:2017
|g number:14
|g day:01
|g month:06
|g pages:3701-3716
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|u http://dx.doi.org/10.1093/jxb/erx110
|3 Volltext
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