Subpicosecond UV spectroscopy of carbonmonoxy-myoglobin: Absorption and circular dichroism studies

Thibault Dartigalongue; Claire Niezborala; François Hache

doi:10.1039/b616173a

Subpicosecond UV spectroscopy of carbonmonoxy-myoglobin: Absorption and circular dichroism studies

Thibault Dartigalongue
, Claire Niezborala
, François Hache

Institut Polytechnique de Paris
University of Toronto

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

Abstract

A thorough absorption and circular dichroism study is performed in carbonmonoxy-myoglobin with a sub-picosecond visible pump, ultraviolet probe experiment. Differential absorption in the 220-360 nm range shows that the time-resolved response mainly comes from the heme and that aromatic amino acids do not contribute significantly. Time-resolved CD at 260 nm shows no dynamics and confirms this result. On the contrary, a strong CD dynamics is observed at 230 nm. This signal could originate from transient deformation of the α-helices in the protein.

Original language	English
Pages (from-to)	1611-1615
Number of pages	5
Journal	Physical Chemistry Chemical Physics
Volume	9
Issue number	13
DOIs	https://doi.org/10.1039/b616173a
Publication status	Published - 19 Apr 2007

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title = "Subpicosecond UV spectroscopy of carbonmonoxy-myoglobin: Absorption and circular dichroism studies",

abstract = "A thorough absorption and circular dichroism study is performed in carbonmonoxy-myoglobin with a sub-picosecond visible pump, ultraviolet probe experiment. Differential absorption in the 220-360 nm range shows that the time-resolved response mainly comes from the heme and that aromatic amino acids do not contribute significantly. Time-resolved CD at 260 nm shows no dynamics and confirms this result. On the contrary, a strong CD dynamics is observed at 230 nm. This signal could originate from transient deformation of the α-helices in the protein.",

author = "Thibault Dartigalongue and Claire Niezborala and Fran{\c c}ois Hache",

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AU - Dartigalongue, Thibault

AU - Niezborala, Claire

AU - Hache, François

PY - 2007/4/19

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N2 - A thorough absorption and circular dichroism study is performed in carbonmonoxy-myoglobin with a sub-picosecond visible pump, ultraviolet probe experiment. Differential absorption in the 220-360 nm range shows that the time-resolved response mainly comes from the heme and that aromatic amino acids do not contribute significantly. Time-resolved CD at 260 nm shows no dynamics and confirms this result. On the contrary, a strong CD dynamics is observed at 230 nm. This signal could originate from transient deformation of the α-helices in the protein.

AB - A thorough absorption and circular dichroism study is performed in carbonmonoxy-myoglobin with a sub-picosecond visible pump, ultraviolet probe experiment. Differential absorption in the 220-360 nm range shows that the time-resolved response mainly comes from the heme and that aromatic amino acids do not contribute significantly. Time-resolved CD at 260 nm shows no dynamics and confirms this result. On the contrary, a strong CD dynamics is observed at 230 nm. This signal could originate from transient deformation of the α-helices in the protein.

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DO - 10.1039/b616173a

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JO - Physical Chemistry Chemical Physics

JF - Physical Chemistry Chemical Physics

IS - 13

ER -

Subpicosecond UV spectroscopy of carbonmonoxy-myoglobin: Absorption and circular dichroism studies

Abstract

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