| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5152628 | Journal of Inorganic Biochemistry | 2017 | 44 Pages |
Abstract
Neisseria gonorrhoeae bacterial peroxidase was heterologously produced in higher yield than previously reported, enabling its biochemical characterization. Specific activity is dependent on reductive activation and calcium, which also modulates redox properties and monomer-dimer equilibrium. This enzyme is highly specific and a first line defense mechanism against exogenously produced hydrogen peroxide.101
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Cláudia S. Nóbrega, Mariana Raposo, Gonzalez Van Driessche, Bart Devreese, Sofia R. Pauleta,