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The Hidden Face of Rubisco

Trends in Plant Science, 2018
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) fixes atmospheric CO2 into organic compounds and is composed of eight copies each of a large subunit (RbcL) and a small subunit (RbcS). Recent reports have revealed unusual RbcS, which are expressed in particular tissues and confer higher catalytic rate, lesser affinity for CO2, and a more ...
Pottier, Mathieu   +2 more
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Rubisco's chiropractor: a study of higher plant Rubisco activase

2015
Rubisco activase operates as the chaperone responsible for maintaining the catalytic competency of Ribulose 1,5-bisphophate carboxylase oxygenase (Rubisco) in plants. Rubisco is notoriously inefficient, rapidly self-inactivating under physiological conditions. Rubisco activase uses the power released from the hydrolysis of ATP to power a conformational
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Evolution and origins of rubisco

Current Biology
Rubisco (D-ribulose 1,5-bisphosphate carboxylase/oxygenase) is the most abundant enzyme in the world, constituting up to half of the soluble protein content in plant leaves. Such is its ubiquity that its chemical fingerprint can be detected in the geological record spanning billions of years.
Leah J, Taylor-Kearney   +2 more
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Purification of Rubisco from Leaves

Rubisco fixes CO2 through the carboxylation of ribulose 1,5-bisphosphate (RuBP) during photosynthesis, enabling the synthesis of organic compounds. The natural diversity of Rubisco properties represents an opportunity to improve its performance and there is considerable research effort focusing on better understanding the properties and regulation of ...
Amaral, Joana   +3 more
openaire   +2 more sources

Rubisco activase

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1990
openaire   +2 more sources

Rubisco

2009
Katia Wostrikoff, David B. Stern
openaire   +1 more source

Rubisco

2020
Cuimin Liu, Kaiyao Huang, Jianrong Xia
openaire   +1 more source

Rubisco

RCSB Protein Data Bank, 2000
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Rubisco

2012
openaire   +1 more source

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