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Originally published as Biophys J. BioFAST on December 30, 2005.
doi:10.1529/biophysj.105.078097
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Biophysical Journal 90:L27-L29 (2006)
© 2006 The Biophysical Society

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

Nikki Strickland, Adrian J. Mulholland and Jeremy N. Harvey

Centre for Computational Chemistry and School of Chemistry, University of Bristol, Bristol, BS8 1TS, United Kingdom

Correspondence: Address reprint requests and inquiries to Jeremy N. Harvey, Tel.: 44-0-117-954 6991; Fax: 44-0-117-925-1295; E-mail: jeremy.harvey{at}bristol.ac.uk.

The Fe-CO bond dissociation energy (BDE) in myoglobin (Mb) has been calculated with B3LYP quantum mechanics/molecular mechanics methods for 22 different Mb conformations, generated from molecular dynamics 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.




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[Abstract] [Full Text] [PDF]


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