Ultrafast 2D-IR spectroscopy of haemoproteins
Simpson, N. and Hunt, N.T. (2015) Ultrafast 2D-IR spectroscopy of haemoproteins. International Reviews in Physical Chemistry, 34 (3). pp. 361-383. ISSN 1366-591X (https://doi.org/10.1080/0144235X.2015.1061793)
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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.
ORCID iDs
Simpson, N. ORCID: https://orcid.org/0000-0003-3139-472X and Hunt, N.T. ORCID: https://orcid.org/0000-0001-7400-5152;-
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Item type: Article ID code: 54125 Dates: DateEvent2015Published13 August 2015Published Online28 May 2015AcceptedNotes: This is an Accepted Manuscript of an article published by Taylor & Francis in International Reviews in Physical Chemistry on 13/08/2015, available online: http://wwww.tandfonline.com/10.1080/0144235X.2015.1061793. Subjects: Science > Physics Department: Faculty of Science > Physics
Technology and Innovation Centre > BionanotechnologyDepositing user: Pure Administrator Date deposited: 02 Sep 2015 08:34 Last modified: 24 Nov 2024 01:10 Related URLs: URI: https://strathprints.strath.ac.uk/id/eprint/54125