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Interaction between Neisseria gonorrhoeae bacterial peroxidase and its electron donor, the lipid‐modified azurin
Author(s) -
Nóbrega Cláudia S.,
Pauleta Sofia R.
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13053
Subject(s) - azurin , chemistry , electron transfer , peroxidase , heme , cytochrome , electron donor , neisseria gonorrhoeae , crystallography , enzyme , catalysis , stereochemistry , biochemistry , photochemistry , biology , microbiology and biotechnology
The Neisseria gonorrhoeae bacterial cytochrome c peroxidase plays a key role in detoxifying the cells from H 2 O 2 by reducing it to water using the lipid‐modified azurin, LAz, a small type 1 copper protein, as electron donor. Here, the interaction between these two proteins was characterized by steady‐state kinetics, two‐dimensional NMR and molecular docking simulations. LA z is an efficient electron donor capable of activating this enzyme. This electron transfer complex is weak with a hydrophobic character, with LA z binding close to the electron transferring heme of the enzyme. The high catalytic rate (39 ± 0.03 s −1 ) is explained by the LA z pre‐orientation, due to a positive dipole moment, and by the fast‐dynamic ensemble of orientations, suggested by the small chemical shifts.