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.
| Original language | English |
|---|---|
| Pages (from-to) | 7411-7419 |
| Number of pages | 9 |
| Journal | Physical Chemistry Chemical Physics |
| Volume | 14 |
| Issue number | 20 |
| Early online date | 29 Mar 2012 |
| DOIs | |
| Publication status | Published - 2012 |
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Keywords
- point mutation
- ferric Myoglobin
- Myoglobin
- NO ligand
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The effect of point mutation on the equilibrium structural fluctuations of ferric Myoglobin. / Adamczyk, Katrin; Candelaresi, Marco; Kania, Rafal; Robb, Kirsty; Bellota-Anton, Cesar; Greetham, Gregory M.; Pollard, Mark R.; Towrie, Michael; Parker, Anthony W.; Hoskisson, Paul A.; Tucker, Nicholas P.; Hunt, Neil T.
In: Physical Chemistry Chemical Physics, Vol. 14, No. 20, 2012, p. 7411-7419.Research output: Contribution to journal › Article
TY - JOUR
T1 - The effect of point mutation on the equilibrium structural fluctuations of ferric Myoglobin
AU - Adamczyk, Katrin
AU - Candelaresi, Marco
AU - Kania, Rafal
AU - Robb, Kirsty
AU - Bellota-Anton, Cesar
AU - Greetham, Gregory M.
AU - Pollard, Mark R.
AU - Towrie, Michael
AU - Parker, Anthony W.
AU - Hoskisson, Paul A.
AU - Tucker, Nicholas P.
AU - Hunt, Neil T.
PY - 2012
Y1 - 2012
N2 - 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.
AB - 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.
KW - point mutation
KW - ferric Myoglobin
KW - Myoglobin
KW - NO ligand
U2 - 10.1039/c2cp23568d
DO - 10.1039/c2cp23568d
M3 - Article
VL - 14
SP - 7411
EP - 7419
JO - Physical Chemistry Chemical Physics
JF - Physical Chemistry Chemical Physics
SN - 1463-9076
IS - 20
ER -