Theoretical characterization of carbon monoxide vibrational spectrum in sperm whale myoglobin distal pocket

Biophys J. 2007 May 15;92(10):3442-7. doi: 10.1529/biophysj.106.098442. Epub 2007 Feb 16.

Abstract

In this article we use the perturbed matrix method and an extended molecular dynamics sampling of the carbon monoxide (CO) in the myoglobin distal pocket to characterize the CO vibrational spectrum and hence to relate its spectroscopic features with the atomic-molecular behavior. Results show the accuracy of the method employed and confirm the assignment of the spectroscopic B1 and B2 states proposed by Lim et al.

MeSH terms

  • Animals
  • Binding Sites
  • Carbon Monoxide / chemistry*
  • Computer Simulation
  • Models, Chemical*
  • Models, Molecular*
  • Myoglobin / chemistry*
  • Protein Binding
  • Protein Conformation
  • Spectrum Analysis
  • Sperm Whale / metabolism*
  • Vibration

Substances

  • Myoglobin
  • Carbon Monoxide