Plug-and-play for improving primary productivity
Abstract
Photosynthesis, the process in which light energy is captured and converted to chemical energy through the Calvin–Benson–Bassham (CBB) cycle is the foundation of the majority of global primary productivity. The first step of the CBB cycle involves the most abundant, and possibly the most problematic protein in the world, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO). The inability of RubisCO to discriminate between CO2 and O2 is considered the key limitation to photosynthetic efficiency; while the carboxylase activity converts CO2 into organic carbon molecules used in biosynthesis, the competing oxygenase activity produces phosphoglycolate, which inhibits some CBB cycle enzymes and must be metabolized via the relatively energetically expensive process of photorespiration. Further, the cost of naturally occurring photorespiratory salvage pathways is compounded by the loss of fixed carbon and nitrogen. Enhancing photosynthesis via remedying the catalytic shortcomings of RuBisCO has long been a major research goal. Despite decades of effort to decrease its oxygenase activity, no work has significantly improved the catalytic properties of RuBisCO. Recent theoretical studies (Tcherkez et al., 2006; Savir et al., 2010) have suggested that RuBisCO may be “nearly perfectly optimized,” possibly explaining the dearth of progress in applying protein engineering to enhance the function RuBisCO. Is it possible tomore »
- Authors:
-
- Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory; Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States); Univ. of California, Berkeley, CA (United States)
- Publication Date:
- Research Org.:
- Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); National Science Foundation (NSF)
- OSTI Identifier:
- 1603342
- Grant/Contract Number:
- FG02-91ER20021
- Resource Type:
- Accepted Manuscript
- Journal Name:
- American Journal of Botany
- Additional Journal Information:
- Journal Volume: 102; Journal Issue: 12; Journal ID: ISSN 0002-9122
- Publisher:
- Wiley - Botanical Society of America
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; modularity; synthetic biology; carboxysome; RuBisCO; photorespiration
Citation Formats
Kerfeld, Cheryl A. Plug-and-play for improving primary productivity. United States: N. p., 2015.
Web. doi:10.3732/ajb.1500409.
Kerfeld, Cheryl A. Plug-and-play for improving primary productivity. United States. https://doi.org/10.3732/ajb.1500409
Kerfeld, Cheryl A. Fri .
"Plug-and-play for improving primary productivity". United States. https://doi.org/10.3732/ajb.1500409. https://www.osti.gov/servlets/purl/1603342.
@article{osti_1603342,
title = {Plug-and-play for improving primary productivity},
author = {Kerfeld, Cheryl A.},
abstractNote = {Photosynthesis, the process in which light energy is captured and converted to chemical energy through the Calvin–Benson–Bassham (CBB) cycle is the foundation of the majority of global primary productivity. The first step of the CBB cycle involves the most abundant, and possibly the most problematic protein in the world, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO). The inability of RubisCO to discriminate between CO2 and O2 is considered the key limitation to photosynthetic efficiency; while the carboxylase activity converts CO2 into organic carbon molecules used in biosynthesis, the competing oxygenase activity produces phosphoglycolate, which inhibits some CBB cycle enzymes and must be metabolized via the relatively energetically expensive process of photorespiration. Further, the cost of naturally occurring photorespiratory salvage pathways is compounded by the loss of fixed carbon and nitrogen. Enhancing photosynthesis via remedying the catalytic shortcomings of RuBisCO has long been a major research goal. Despite decades of effort to decrease its oxygenase activity, no work has significantly improved the catalytic properties of RuBisCO. Recent theoretical studies (Tcherkez et al., 2006; Savir et al., 2010) have suggested that RuBisCO may be “nearly perfectly optimized,” possibly explaining the dearth of progress in applying protein engineering to enhance the function RuBisCO. Is it possible to overcome the limitations in the product of billions of years of evolution?},
doi = {10.3732/ajb.1500409},
journal = {American Journal of Botany},
number = 12,
volume = 102,
place = {United States},
year = {Fri Dec 11 00:00:00 EST 2015},
month = {Fri Dec 11 00:00:00 EST 2015}
}
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