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Lack of proton-pumping activity has also been found in heterologously expressed Neurospora rhodopsin, which has carboxylated residues at both the Schiff base proton donor and acceptor positions, as does GtR1.
As the name of the enzyme implies, pyruvate is carboxylated to form oxaloacetate.
Depending on ratios of CO 2 to O 2 at binding sites of ribulose bisphosphate carboxylase, ribulose bisphosphate is either carboxylated or oxygenated.
The optically trapped carboxylated bead is attached to the cationic vesicle adhered onto a glass coverslip, by electrostatic interactions.
It is suggested that mitochondrial pyruvate is partly oxidized by the TCA cycle and is partly exported to the cytoplasm where it is carboxylated to form malate 1-for continued export to the apoplast.
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