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Title: Structural studies of proteins involved in carbon fixation
Author: Kabasakal, Burak Veli
ISNI:       0000 0004 9350 0820
Awarding Body: Imperial College London
Current Institution: Imperial College London
Date of Award: 2017
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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.
Supervisor: Murray, James William Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral