Jump to main content
Jump to site search

Issue 20, 2012
Previous Article Next Article

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

Author affiliations

Abstract

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.

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

Back to tab navigation

Supplementary files

Publication details

The article was received on 12 Nov 2011, accepted on 28 Mar 2012 and first published on 29 Mar 2012


Article type: Paper
DOI: 10.1039/C2CP23568D
Citation: Phys. Chem. Chem. Phys., 2012,14, 7411-7419
  •   Request permissions

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

    K. Adamczyk, M. Candelaresi, R. Kania, K. Robb, C. Bellota-Antón, G. M. Greetham, M. R. Pollard, M. Towrie, A. W. Parker, P. A. Hoskisson, N. P. Tucker and N. T. Hunt, Phys. Chem. Chem. Phys., 2012, 14, 7411
    DOI: 10.1039/C2CP23568D

Search articles by author

Spotlight

Advertisements