Ultrafast 2D-IR spectroscopy of haemoproteins

N. Simpson, N.T. Hunt

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Applications of ultrafast two-dimensional infrared (2D-IR) spectroscopy to study the structural dynamics of haem-containing proteins are reviewed. The 2D-IR experiments discussed exploit diatomic ligands bound to the haem as reporters on the dynamic protein environment in the electronic ground-state. This is possible because fluctuations of the protein give rise to inhomogeneous broadening of the ligand stretching vibrational mode that is manifest as spectral diffusion in a time-resolved 2D-IR measurement. Methods for measuring and quantifying spectral diffusion data are introduced, prior to a discussion of recent results focussing on the influence of protein structure, water ingress into the haem pocket and substrate binding on the measured dynamics. Particular emphasis will be placed on proteins featuring the ferric oxidation state of the haem ligated by a nitric oxide molecule, though comparisons with other haem systems will be drawn throughout.
LanguageEnglish
Pages361-383
Number of pages23
JournalInternational Reviews in Physical Chemistry
Volume34
Issue number3
Early online date13 Aug 2015
DOIs
Publication statusPublished - 2015

Fingerprint

Heme
Infrared spectroscopy
proteins
spectroscopy
Proteins
Ligands
ligands
dynamic structural analysis
Structural dynamics
nitric oxide
Ground state
Stretching
vibration mode
Nitric Oxide
Oxidation
oxidation
Molecules
ground state
Water
Substrates

Keywords

  • ultrafast
  • infrared
  • 2D IR spectroscopy
  • haem
  • protein dynamics

Cite this

Simpson, N. ; Hunt, N.T. / Ultrafast 2D-IR spectroscopy of haemoproteins. In: International Reviews in Physical Chemistry. 2015 ; Vol. 34, No. 3. pp. 361-383.
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Ultrafast 2D-IR spectroscopy of haemoproteins. / Simpson, N.; Hunt, N.T.

In: International Reviews in Physical Chemistry, Vol. 34, No. 3, 2015, p. 361-383.

Research output: Contribution to journalArticle

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AU - Hunt, N.T.

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AB - Applications of ultrafast two-dimensional infrared (2D-IR) spectroscopy to study the structural dynamics of haem-containing proteins are reviewed. The 2D-IR experiments discussed exploit diatomic ligands bound to the haem as reporters on the dynamic protein environment in the electronic ground-state. This is possible because fluctuations of the protein give rise to inhomogeneous broadening of the ligand stretching vibrational mode that is manifest as spectral diffusion in a time-resolved 2D-IR measurement. Methods for measuring and quantifying spectral diffusion data are introduced, prior to a discussion of recent results focussing on the influence of protein structure, water ingress into the haem pocket and substrate binding on the measured dynamics. Particular emphasis will be placed on proteins featuring the ferric oxidation state of the haem ligated by a nitric oxide molecule, though comparisons with other haem systems will be drawn throughout.

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