collection
MENU ▼
Read by QxMD icon Read
search

Rubisco

shared collection
3 papers 25 to 100 followers
https://www.readbyqxmd.com/read/21953262/nanoesi-mass-spectrometry-of-rubisco-and-rubisco-activase-structures-and-their-interactions-with-nucleotides-and-sugar-phosphates
#1
Michelle J Blayney, Spencer M Whitney, Jennifer L Beck
Ribulose bisphosphate carboxylase/oxygenase (Rubisco) is the protein that is responsible for the fixation of carbon dioxide in photosynthesis. Inhibitory sugar phosphate molecules, which can include its substrate ribulose-1,5-bisphosphate (RuBP), can bind to Rubisco catalytic sites and inhibit catalysis. These are removed by interaction with Rubisco activase (RA) via an ATP hydrolytic reaction. Here we show the first nanoESI mass spectra of the hexadecameric Rubisco and of RA from a higher plant (tobacco). The spectra of recombinant, purified RA revealed polydispersity in its oligomeric forms (up to hexamer) and that ADP was bound...
September 2011: Journal of the American Society for Mass Spectrometry
https://www.readbyqxmd.com/read/24495214/co2-and-o2-distribution-in-rubisco-suggests-the-small-subunit-functions-as-a-co2-reservoir
#2
Michiel van Lun, Jochen S Hub, David van der Spoel, Inger Andersson
Protein-gas interactions are important in biology. The enzyme ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes two competing reactions involving CO2 and O2 as substrates. Carboxylation of the common substrate ribulose-1,5-bisphosphate leads to photosynthetic carbon assimilation, while the oxygenation reaction competes with carboxylation and reduces photosynthetic productivity. The migration of the two gases in and around Rubisco was investigated using molecular dynamics simulations. The results indicate that at equal concentrations of the gases, Rubisco binds CO2 stronger than it does O2...
February 26, 2014: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/23112176/structural-mechanism-of-rubisco-activation-by-carbamylation-of-the-active-site-lysine
#3
Boguslaw Stec
Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is a crucial enzyme in carbon fixation and the most abundant protein on earth. It has been studied extensively by biochemical and structural methods; however, the most essential activation step has not yet been described. Here, we describe the mechanistic details of Lys carbamylation that leads to RuBisCO activation by atmospheric CO(2). We report two crystal structures of nitrosylated RuBisCO from the red algae Galdieria sulphuraria with O(2) and CO(2) bound at the active site...
November 13, 2012: Proceedings of the National Academy of Sciences of the United States of America
1
Fetch more papers »
Fetching more papers... Fetching...
Read by QxMD. Sign in or create an account to discover new knowledge that matter to you.
Remove bar
Read by QxMD icon Read
×

Search Tips

Use Boolean operators: AND/OR

diabetic AND foot
diabetes OR diabetic

Exclude a word using the 'minus' sign

Virchow -triad

Use Parentheses

water AND (cup OR glass)

Add an asterisk (*) at end of a word to include word stems

Neuro* will search for Neurology, Neuroscientist, Neurological, and so on

Use quotes to search for an exact phrase

"primary prevention of cancer"
(heart or cardiac or cardio*) AND arrest -"American Heart Association"