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Biophys. J. BioFAST: First Published December 30, 2005. doi:10.1529/biophysj.105.078097
© 2005 by the Biophysical Society.

A more recent version of this article appeared on February 15, 2006.
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BIOPHYSICAL LETTERS

The Fe-CO Bond Energy in Myoglobin: A QM/MM Study of the Effect of Tertiary Structure

Nikki Strickland 1, Adrian J Mulholland 1 and Jeremy N Harvey 1*

1 University of Bristol

* To whom correspondence should be addressed. E-mail: jeremy.harvey{at}bris.ac.uk.

Submitted on November 18, 2005
Revised on November 30, 2005
Accepted on 13 December 2005


  Abstract
The Fe-CO Bond Dissociation Energy (BDE) in myoglobin (Mb)has been calculated with B3LYP quantum mechanics/molecular mechanics (QM/MM) methods for 22 different Mb conformations, generated from molecular dynamics (MD) simulations. Our average BDE of 8.1 kcal/mol agrees well with experiment and shows that Mb weakens the Fe-CO bond by 5.8 kcal/mol; the calculations provide detailed atomistic insight into the origin of this effect. BDEs for Mb conformations with the R carbonmonoxy tertiary structure are on average 2.6 kcal/mol larger than those with the T deoxy tertiary structure, suggesting two functionally distinct allosteric states. This allostery is partly explained by the reduction in distal cavity steric crowding as Mb moves from its T to R tertiary structure.

Key Words: Allosteric Effects, Bond Energy, Computation, Myoglobin, QM/MM




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[Abstract] [Full Text] [PDF]


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Copyright © 2005 by the Biophysical Society.