T
T. John Andrews
Researcher at Australian National University
Publications - 44
Citations - 4165
T. John Andrews is an academic researcher from Australian National University. The author has contributed to research in topics: RuBisCO & Photosynthesis. The author has an hindex of 27, co-authored 44 publications receiving 3890 citations. Previous affiliations of T. John Andrews include Australian Institute of Marine Science.
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Journal ArticleDOI
Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized.
TL;DR: It is asserted that all Rubiscos may be nearly perfectly adapted to the differing CO(2, O(2), and thermal conditions in their subcellular environments, optimizing this compromise between CO( 2)/O(2) specificity and the maximum rate of catalytic turnover.
Journal ArticleDOI
The diversity and coevolution of rubisco, plastids, pyrenoids, and chloroplast-based co2-concentrating mechanisms in algae
Murray R. Badger,T. John Andrews,Spencer M. Whitney,Martha Ludwig,David Yellowlees,William Leggat,G. Dean Price +6 more
TL;DR: This review examines the potential diversity of both Rubisco and chloroplast-based CCMs across algal divisions, including both green and nongreen algae, and seeks to highlight recent advances in the understanding of the area and future areas for research.
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The kinetics of ribulose-1,5-bisphosphate carboxylase/oxygenase in vivo inferred from measurements of photosynthesis in leaves of transgenic tobacco
TL;DR: Transgenic tobacco with an antisense gene directed against the mRNA of the ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) small subunit was used to determine the kinetic properties of Rubisco in vivo, and Rubisco's relative specificity for CO2 was estimated to be 97.5 in vivo.
Journal ArticleDOI
Reduction of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Content by Antisense RNA Reduces Photosynthesis in Transgenic Tobacco Plants
TL;DR: Results suggest that stomatal function is independent of total leaf Rubisco activity and that carbon isotope discrimination in the leaves of the antisense plants is greater than in control leaves.
Journal ArticleDOI
Faster Rubisco is the key to superior nitrogen-use efficiency in NADP-malic enzyme relative to NAD-malic enzyme C4 grasses.
Oula Ghannoum,John R. Evans,Wah Soon Chow,T. John Andrews,Jann P Conroy,Susanne von Caemmerer +5 more
TL;DR: In conclusion, superior N-use efficiency of NADP-ME relative to NAD-ME grasses was achieved with less leaf N, soluble protein, and Rubisco having a faster kcat.