Inhibition of ferric ion to oxalate oxidase shed light on the substrate binding site
| Autor: | Wanjun Lan, Xuelei Huang, Guanke Zuo, Jingyan Zhang, Hui Liu, Yu Pang |
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| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular inorganic chemicals Oxalate oxidase Iron Inorganic chemistry Catalysis Protein Structure Secondary General Biochemistry Genetics and Molecular Biology Oxalate Substrate Specificity Biomaterials chemistry.chemical_compound Binding site Hydrogen peroxide Protein secondary structure Ions chemistry.chemical_classification Binding Sites Microscale thermophoresis Circular Dichroism Metals and Alloys Hydrogen Peroxide Combinatorial chemistry Molecular Docking Simulation Oxygen Enzyme chemistry Docking (molecular) Oxidoreductases General Agricultural and Biological Sciences |
| Zdroj: | BioMetals. 28:861-868 |
| ISSN: | 1572-8773 0966-0844 |
| DOI: | 10.1007/s10534-015-9871-7 |
| Popis: | Oxalate oxidase (OxOx), a well known enzyme catalyzes the cleavage of oxalate to carbon dioxide with reduction of dioxygen to hydrogen peroxide, however its catalytic process is not well understood. To define the substrate binding site, interaction of Fe(3+) ions with OxOx was systemically investigated using biochemical method, circular dichrosim spectroscopy, microscale thermophoresis, and computer modeling. We demonstrated that Fe(3+) is a non-competitive inhibitor with a milder binding affinity to OxOx, and the secondary structure of the OxOx was slightly altered upon its binding. On the basis of the structural properties of the OxOx and its interaction with Fe(3+) ions, two residue clusters of OxOx were assigned as potential Fe(3+) binding sites, the mechanism of the inhibition of Fe(3+) was delineated. Importantly, the residues that interact with Fe(3+) ions are involved in the substrate orienting based on computer docking. Consequently, the interaction of OxOx with Fe(3+) highlights insight into substrate binding site in OxOx. |
| Databáze: | OpenAIRE |
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