The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Distinct form I, II, III, and IV Rubisco proteins from the three kingdoms of life provide clues about Rubisco evolution and structure/function relationships
Abstract
There are four forms of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) found in nature. Forms I, II, and III catalyse the carboxylation and oxygenation of ribulose 1,5-bisphosphate, while form IV, also called the Rubisco-like protein (RLP), does not catalyse either of these reactions. There appear to be six different clades of RLP. Although related to bona fide Rubisco proteins at the primary sequence and tertiary structure levels, RLP from two of these clades is known to perform other functions in the cell. Forms I, II, and III Rubisco, along with form IV (RLP), are thought to have evolved from a primordial archaeal Rubisco. Structure/function studies with both archaeal form III (methanogen) and form I (cyanobacterial) Rubisco have identified residues that appear to be specifically involved with interactions with molecular oxygen. A specific region of all form I, II, and III Rubisco was identified as being important for these interactions.
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Cites
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Self-citationMicrobial ribulose 1,5-bisphosphate carboxylase/oxygenase: A different perspective
Tabita, F. R. (1999) · Photosynthesis Research · doi:10.1023/a:1006211417981 · Cited by 365
Self-citationSTRUCTURE, FUNCTION, REGULATION, AND ASSEMBLY OF D-RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE
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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
Beyond the Calvin Cycle: Autotrophic Carbon Fixation in the Ocean
Hügler, M., & Sievert, S. M. (2011) · Annual Review of Marine Science · doi:10.1146/annurev-marine-120709-142712 · Cited by 686
Structure 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
Genomic insights into the uncultivated marine Zetaproteobacteria at Loihi Seamount
Field, E. K., Sczyrba, A., Lyman, A. E., Harris, C. C., Woyke, T., Stepanauskas, R., & Emerson, D. (2015) · The ISME Journal · doi:10.1038/ismej.2014.183 · Cited by 79
Rubisco Adaptation Is More Limited by Phylogenetic Constraint Than by Catalytic Trade-off
Bouvier, J. W., Emms, D. M., Rhodes, T., Bolton, J. S., Brasnett, A., Eddershaw, A., Nielsen, J. R., Unitt, A., Whitney, S. M., & Kelly, S. (2021) · Molecular Biology and Evolution · doi:10.1093/molbev/msab079 · Cited by 65
Metadata
- Authors
- Tabita, F. R., Satagopan, S., Hanson, T. E., Kreel, N. E., & Scott, S. S.
- Venue
- Journal of Experimental Botany
- Publisher
- Oxford University Press (OUP)
- Published
- 2007-06-19
- Volume
- 59
- Issue
- 7
- Pages
- 1515-1524
- ISSN
- 0022-0957 (ISSN-L)
- 1460-2431
- OpenAlex
- W2098840374
- Cited by
- 414
- References
- 35
- FWCI
- 2.39
- Type
- journal article
- Language
- en
- Open access
- closed
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- Tabita, F. R., Satagopan, S., Hanson, T. E., Kreel, N. E., & Scott, S. S. (2007). Distinct form I, II, III, and IV Rubisco proteins from the three kingdoms of life provide clues about Rubisco evolution and structure/function relationships. Journal of Experimental Botany. https://doi.org/10.1093/jxb/erm361
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