The effect of point mutation on the equilibrium structural fluctuations of ferric Myoglobin

Katrin Adamczyk, Marco Candelaresi, Rafal Kania, Kirsty Robb, Cesar Bellota-Anton, Gregory M. Greetham, Mark R. Pollard, Michael Towrie, Anthony W. Parker, Paul A. Hoskisson, Nicholas P. Tucker, Neil T. Hunt

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20 Citations (Scopus)


The ultrafast equilibrium fluctuations of the FeIII-NO complex of a single point mutation of Myoglobin (H64Q) have been studied using Fourier Transform 2D-IR spectroscopy. Comparison with data from wild type Myoglobin (wt-Mb) shows the presence of two
conformational substates of the mutant haem pocket where only one exists in the wild type form. One of the substates of the mutant exhibits an almost identical NO stretching frequency and spectral diffusion dynamics to wt-Mb while the other is distinctly different in both respects. The remarkably contrasting dynamics are largely attributable to interactions
between the NO ligand and a nearby distal side chain which provides a basis for understanding the roles of these side chains in other ferric haem proteins.

Original languageEnglish
Pages (from-to)7411-7419
Number of pages9
JournalPhysical Chemistry Chemical Physics
Issue number20
Early online date29 Mar 2012
Publication statusPublished - 2012



  • point mutation
  • ferric Myoglobin
  • Myoglobin
  • NO ligand

Cite this

Adamczyk, K., Candelaresi, M., Kania, R., Robb, K., Bellota-Anton, C., Greetham, G. M., ... Hunt, N. T. (2012). The effect of point mutation on the equilibrium structural fluctuations of ferric Myoglobin. Physical Chemistry Chemical Physics, 14(20), 7411-7419.