The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Multiple Rubisco forms in proteobacteria: their functional significance in relation to CO2 acquisition by the CBB cycle
Open accessAbstract
Rubisco is the predominant enzymatic mechanism in the biosphere by which autotrophic bacteria, algae, and terrestrial plants fix CO(2) into organic biomass via the Calvin-Benson-Basham reductive pentose phosphate pathway. Rubisco is not a perfect catalyst, suffering from low turnover rates, a low affinity for its CO(2) substrate, and a competitive inhibition by O(2) as an alternative substrate. As a consequence of changing environmental conditions over the past 3.5 billion years, with decreasing CO(2) and increasing O(2) in the atmosphere, Rubisco has evolved into multiple enzymatic forms with a range of kinetic properties, as well as co-evolving with CO(2)-concentrating mechanisms to cope with the different environmental contexts in which it must operate. The most dramatic evidence of this is the occurrence of multiple forms of Rubisco within autotrophic proteobacteria, where Forms II, IC, IBc, IAc, and IAq can be found either singly or in multiple combinations within a particular bacterial genome. Over the past few years there has been increasing availability of genomic sequence data for bacteria and this has allowed us to gain more extensive insights into the functional significance of this diversification. This paper is focused on summarizing what is known about the diversity of Rubisco forms, their kinetic properties, development of bacterial CO(2)-concentrating mechanisms, and correlations with metabolic flexibility and inorganic carbon environments in which proteobacteria perform various types of obligate and facultative chemo- and photoautotrophic CO(2) fixation.
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Cites
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GEOCARB III: A revised model of atmospheric CO2 over Phanerozoic time
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R UBISCO : Structure, Regulatory Interactions, and Possibilities for a Better Enzyme
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CO2 concentrating mechanisms in cyanobacteria: Molecular components, their diversity and evolution
Badger, M. R. (2003) · Journal of Experimental Botany · doi:10.1093/jxb/erg076 · Cited by 841
Self-citationTcherkez, G. G. B., Farquhar, G. D., & Andrews, T. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600605103 · Cited by 770
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Mechanism of Rubisco: the carbamate as general base
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Cited by
Ecological Aspects of the Distribution of Different Autotrophic CO 2 Fixation Pathways
Berg, I. A. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.02473-10 · Cited by 821
Rae, B. D., Long, B. M., Badger, M. R., & Price, G. D. (2013) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00061-12 · Cited by 409
Self-citationStructure and function of the AAA+ protein CbbX, a red-type Rubisco activase
Mueller-Cajar, O., Stotz, M., Wendler, P., Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10568 · Cited by 190
Jan, C., Petersen, J. M., Werner, J., Teeling, H., Huang, S., Glöckner, F. O., Golyshina, O. V., Dubilier, N., Golyshin, P. N., Jebbar, M., et al. (2014) · Environmental Microbiology · doi:10.1111/1462-2920.12406 · Cited by 83
Hügler, M., Petersen, J. M., Dubilier, N., Imhoff, J. F., & Sievert, S. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016018 · Cited by 80
Metadata
- Authors
- Badger, M. R., & Bek, E. J.
- Venue
- Journal of Experimental Botany
- Publisher
- Oxford University Press (OUP)
- Published
- 2008-02-02
- Volume
- 59
- Issue
- 7
- Pages
- 1525-1541
- ISSN
- 0022-0957 (ISSN-L)
- 1460-2431
- OpenAlex
- W2163066505
- Cited by
- 434
- References
- 48
- FWCI
- 5.34
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Badger, M. R., & Bek, E. J. (2008). Multiple Rubisco forms in proteobacteria: their functional significance in relation to CO2 acquisition by the CBB cycle. Journal of Experimental Botany. https://doi.org/10.1093/jxb/erm297
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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