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Full-Text Articles in Biochemistry, Biophysics, and Structural Biology
Investigating The Role Of The Proximal Cysteine Hydrogen Bonding Network And Distal Pocket In Chloroperoxidase, Elwood Kwong Lam
Investigating The Role Of The Proximal Cysteine Hydrogen Bonding Network And Distal Pocket In Chloroperoxidase, Elwood Kwong Lam
FIU Electronic Theses and Dissertations
Chloroperoxidase (CPO) is one of the most versatile heme enzyme isolated from the marine fungus, Caldariomyces fumago. Functionally, CPO can catalyze four types of reactions: peroxidation (peroxidase-like), dismutation (catalase-like), halogenation (halogenase-like), and peroxygenation (P450-like). Structurally, CPO has a distal and proximal pockets that can be best described as a hybrid of classical peroxidase and P450s. As a heme-thiolate protein, CPO contains the conserved proximal Pro28-Cys29-Pro30 stretch found in other members of the family. However, the structural and functional roles of these proline residues remain poorly understood. Site-directed mutagenesis was undertaken to generates three CPO mutants, P28A-, P30A-, P28A/P30A-CPO. The replacement …
The Influence Of The Proximal Thiolate Ligand And Hydrogen Bond Network Of The Proximal Helix On The Structural And Biochemical Properties Of Chloroperoxidase, Elena Shersher
FIU Electronic Theses and Dissertations
Chloroperoxidase (CPO) from Caldariomyces fumago is a versatile heme enzyme with great potential for environmental and pharmaceutical applications. It catalyzes a plethora of reactions including halogenation, dismutation, epoxidation, and oxidation. The diverse catalytic capabilities of CPO have long been attributed to the protein’s distinct active site that combines structural features of peroxidases and cytochromes P450. Particularly, the role of the axial thiolate ligand in CPO catalysis has been much debated. Furthermore, no data are available on the role of hydrogen bonding between Arg 26-Asn 37 and Ala 27-Asn 33 of the proximal helix in defining the structural and catalytic properties …