Jump to main content
Jump to site search

Volume 148, 2011
Previous Article Next Article

Theoretical simulation of the spectroscopy and dynamics of a red copper protein

Author affiliations

Abstract

The electronic absorption, circular dichroism and X-ray absorption spectroscopy of the red copper protein nitrosocyanin is simulated with classical molecular dynamics simulations in conjunction with time-dependent density functional theory (TDDFT) and multireference configuration interaction (MRCI) calculations on the active site, with the remainder of the protein and solvent included via point charges. In the molecular dynamics simulations of the oxidised form of the protein an exogenous water coordinates with the copper centre. Both TDDFT and MRCI approaches predict accurate excitation energies and give qualitatively correct absorption spectra. The most significant discrepancy with experiment is an underestimation of the intensity for the Cysπ band. Circular dichroism spectra are more difficult to compute accurately, and the best agreement with experiment is found using the velocity formulation for the rotational strength. However, this predicts the Cysσ band with an incorrect sign. In the X-ray region, TDDFT in conjunction with a short-range corrected functional provides an accurate description of the pre-edge features at the copper and sulfur K-edges.

Back to tab navigation

Publication details

The article was received on 12 Mar 2010, accepted on 06 Apr 2010 and first published on 20 Aug 2010


Article type: Paper
DOI: 10.1039/C004231E
Citation: Faraday Discuss., 2011,148, 55-70
  •   Request permissions

    Theoretical simulation of the spectroscopy and dynamics of a red copper protein

    N. A. Besley and D. Robinson, Faraday Discuss., 2011, 148, 55
    DOI: 10.1039/C004231E

Search articles by author

Spotlight

Advertisements