Carme Rovira 2003 J. Phys.: Condens. Matter 15 S1809 doi:10.1088/0953-8984/15/18/314
Carme Rovira
Show affiliationsThis paper is a review of our recent work on the structure and dynamics of the Fe–CO bond in carbonmonoxy myoglobin (MbCO), performed using density functional theory, Car–Parrinello molecular dynamics and hybrid quantum mechanics/molecular mechanics approaches. The results of these investigations have served to shed light onto one of the long standing questions in myoglobin research: whether the protein discriminates the CO ligand with respect to O2 by distorting the FeCO bond. The calculations show that both in the gas phase and in the protein the Fe–CO bond is essentially linear and therefore exclude the hypothesis that the CO in MbCO is sterically hindered. In contrast, hydrogen bonding between the O2 ligand and the His64 residue easily explains the protein discrimination for CO.
87.15.K- Molecular interactions; membrane-protein interactions
87.15.B- Structure of biomolecules
Issue 18 (14 May 2003)
Received 11 October 2002
Published 28 April 2003
Carme Rovira 2003 J. Phys.: Condens. Matter 15 S1809
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