Interaction between Neisseria gonorrhoeae bacterial peroxidase and its electron donor, the lipid-modified azurin

Research output: Contribution to journalLetter

2 Citations (Scopus)
1 Downloads (Pure)

Abstract

The Neisseria gonorrhoeae bacterial cytochrome c peroxidase plays a key role in detoxifying the cells from H2O2 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. LAz is an efficient electron donor capable of activating this enzyme. This electron transfer complex is weak with a hydrophobic character, with LAz binding close to the electron transferring heme of the enzyme. The high catalytic rate (39 ± 0.03 s−1) is explained by the LAz pre-orientation, due to a positive dipole moment, and by the fast-dynamic ensemble of orientations, suggested by the small chemical shifts.

Original languageEnglish
Pages (from-to)1473-1483
Number of pages11
JournalFEBS Letters
Volume592
Issue number9
DOIs
Publication statusPublished - 1 May 2018

Keywords

  • bacterial cytochrome c peroxidase
  • electron transfer pathway
  • lipid-modified azurin
  • molecular docking
  • Neisseria gonorrhoeae
  • protein–protein interaction

Fingerprint Dive into the research topics of 'Interaction between Neisseria gonorrhoeae bacterial peroxidase and its electron donor, the lipid-modified azurin'. Together they form a unique fingerprint.

Cite this