Documentation scienceplus.abes.fr version Bêta

À propos de : Hydrogen Bonding in the Blue-Copper Site. Resonance Raman Study        

AttributsValeurs
type
Is Part Of
Subject
Title
  • Hydrogen Bonding in the Blue-Copper Site. Resonance Raman Study
has manifestation of work
related by
Author
Abstract
  • The blue-copper proteins azurin from Pseudomonas aeruginosa, azurin from Alcaligenes denitrificans, andthe mutant Met121Gln of azurin from Alcaligenes denitrificans have been investigated by resonance Ramanspectroscopy. Large deuterium isotope shifts up to 6 cm-1 have been observed for bands in the 350−460cm-1 range after incubation of the apoproteins in D2O and subsequent reconstitution with copper. The shiftsderive from the deuteration of the amide hydrogens of Asn47 and Phe114 that form a hydrogen bond withthe sulfur of the copper-coordinated cysteine. This observation reveals the coupling of the copper−sulfur andsulfur−hydrogen vibrations and indicates that these amide groups have to be taken into account to properlydescribe the electronic structure of the blue-copper site.
article type
is part of this journal



Alternative Linked Data Documents: ODE     Content Formats:       RDF       ODATA       Microdata