Constant pH Accelerated Molecular Dynamics Investigation of the pH Regulation Mechanism of Dinoflagellate Luciferase
| Autor: | Steven O. Mansoorabadi, Patrick H. Donnan, Phong D. Ngo |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Protein Conformation Molecular Dynamics Simulation 01 natural sciences Biochemistry 03 medical and health sciences chemistry.chemical_compound Protein structure Bioluminescence Luciferase Luciferases Histidine chemistry.chemical_classification biology 010405 organic chemistry Chemistry Hydrogen bond Dinoflagellate Hydrogen Bonding Hydrogen-Ion Concentration biology.organism_classification Tetrapyrrole 0104 chemical sciences 030104 developmental biology Enzyme Luminescent Measurements Dinoflagellida Acids |
| Zdroj: | Biochemistry. 57:295-299 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/acs.biochem.7b00873 |
| Popis: | The bioluminescence reaction in dinoflagellates involves the oxidation of an open-chain tetrapyrrole by the enzyme dinoflagellate luciferase (LCF). The activity of LCF is tightly regulated by pH, where the enzyme is essentially inactive at pH ∼8 and optimally active at pH ∼6. Little is known about the mechanism of LCF or the structure of the active form of the enzyme, although it has been proposed that several intramolecularly conserved histidine residues in the N-terminal region are important for the pH regulation mechanism. Here, constant pH accelerated molecular dynamics was employed to gain insight into the conformational activation of LCF induced by acidification. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|