Pseudoazurin-nitrite reductase interactions

Antonietta Impagliazzo, Ludwig Krippahl, Marcellus Ubbink

Research output: Contribution to journalArticlepeer-review

15 Citations (Scopus)

Abstract

The nitrite reductase-binding site on pseudoazurin has been determined by using NMR chemical-shift perturbations. It comprises residues in the hydrophobic patch surrounding the exposed copper ligand His81 as well as several positively charged residues. The binding site is similar for both redox states of pseudoazurin, despite differences in the binding mode. The results suggest that pseudoazurin binds in a well-defined orientation. Docking simulations provide a putative structure of the complex with a binding site on nitrite reductase that has several hydrophobic and polar residues as well as a ridge of negatively charged side chains and a copper-to-copper distance of 14 Å.

Original languageEnglish
Pages (from-to)1648-1653
Number of pages6
JournalChembiochem
Volume6
Issue number9
DOIs
Publication statusPublished - Sep 2005

Keywords

  • Electron transfer
  • Metalloproteins
  • Nitrite reductase
  • NMR spectroscopy
  • Pseudoazurin

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