Structural studies of proteins involved in carbon fixation
File(s)
Author(s)
Kabasakal, Burak Veli
Type
Thesis
Abstract
In this thesis, the structures of proteins involved in carbon fixation by enzymes of the 3 hydroxypropionate (3 HP) cycle of Chloroflexus aurantiacus, and the acetone carboxylase from Xanthobacter autrophicus were investigated. The crystal structures of C-terminal and N-terminal domains of malonyl CoA reductase, and mesaconyl C1-CoA hydratase were solved. Preliminary structural information was obtained for mesaconyl-CoA transferase and mesaconyl-C4-CoA hydratase, the right-hand side 3 HP cycle enzymes. The mechanism of 3 HP formation from malonyl CoA, catalysed by malonyl CoA reductase was studied using ligand bound structures, site-directed mutagenesis, and kinetics.
The ATP dependent acetone carboxylation mechanism was examined structurally. Acetone carboxylase was natively purified from Xanthobacter autotrophicus and the AMP and acetate bound structure was determined at 1.9 Å. This thesis has applications in the biotechnology of carbon fixation.
The ATP dependent acetone carboxylation mechanism was examined structurally. Acetone carboxylase was natively purified from Xanthobacter autotrophicus and the AMP and acetate bound structure was determined at 1.9 Å. This thesis has applications in the biotechnology of carbon fixation.
Version
Open Access
Date Issued
2017-09
Date Awarded
2018-04
Advisor
Murray, James William
Publisher Department
Life Sciences
Publisher Institution
Imperial College London
Qualification Level
Doctoral
Qualification Name
Doctor of Philosophy (PhD)