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

doi:10.1039/c2cp23568d

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

Research output: Contribution to journal › Article › peer-review

21 Citations (Scopus)

Abstract

The ultrafast equilibrium fluctuations of the Fe^III-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	https://doi.org/10.1039/c2cp23568d
Publication status	Published - 2012

Keywords

point mutation
ferric Myoglobin
Myoglobin
NO ligand

Access to Document

10.1039/c2cp23568d

Cite this

@article{bf32b920e2414e138f83bbbba03ec1dd,

title = "The effect of point mutation on the equilibrium structural fluctuations of ferric Myoglobin",

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.",

keywords = "point mutation , ferric Myoglobin , Myoglobin , NO ligand",

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

year = "2012",

doi = "10.1039/c2cp23568d",

language = "English",

volume = "14",

pages = "7411--7419",

journal = "Physical Chemistry Chemical Physics",

issn = "1463-9076",

publisher = "Royal Society of Chemistry",

number = "20",

}

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 -

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

Abstract

Keywords

Access to Document

Fingerprint

Cite this