Observation of sub-100 ps conformational changes in photolyzed carbonmonoxy-myoglobin probed by time-resolved circular dichroism

Thibault Dartigalongue; François Hache

doi:10.1016/j.cplett.2005.09.022

Observation of sub-100 ps conformational changes in photolyzed carbonmonoxy-myoglobin probed by time-resolved circular dichroism

Thibault Dartigalongue
, François Hache

Institut Polytechnique de Paris

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

Abstract

A time-resolved circular dichroism (CD) experiment is carried out on carbonmonoxy-myoglobin. The CD is measured with a sub-picosecond time resolution after ligand dissociation and the data are interpreted thanks to a classical CD calculation based on the polarizability theory. We observe a decrease of the CD signal in a few picoseconds and a sub-100 ps relaxation towards steady-state deoxy-myoglobin values which we assign to a stress of the proximal histidine which relaxes with the global reorganization of the protein from its liganded geometry to its deliganded one.

Original language	English
Pages (from-to)	313-316
Number of pages	4
Journal	Chemical Physics Letters
Volume	415
Issue number	4-6
DOIs	https://doi.org/10.1016/j.cplett.2005.09.022
Publication status	Published - 11 Nov 2005

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10.1016/j.cplett.2005.09.022

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title = "Observation of sub-100 ps conformational changes in photolyzed carbonmonoxy-myoglobin probed by time-resolved circular dichroism",

abstract = "A time-resolved circular dichroism (CD) experiment is carried out on carbonmonoxy-myoglobin. The CD is measured with a sub-picosecond time resolution after ligand dissociation and the data are interpreted thanks to a classical CD calculation based on the polarizability theory. We observe a decrease of the CD signal in a few picoseconds and a sub-100 ps relaxation towards steady-state deoxy-myoglobin values which we assign to a stress of the proximal histidine which relaxes with the global reorganization of the protein from its liganded geometry to its deliganded one.",

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

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AU - Dartigalongue, Thibault

AU - Hache, François

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Y1 - 2005/11/11

N2 - A time-resolved circular dichroism (CD) experiment is carried out on carbonmonoxy-myoglobin. The CD is measured with a sub-picosecond time resolution after ligand dissociation and the data are interpreted thanks to a classical CD calculation based on the polarizability theory. We observe a decrease of the CD signal in a few picoseconds and a sub-100 ps relaxation towards steady-state deoxy-myoglobin values which we assign to a stress of the proximal histidine which relaxes with the global reorganization of the protein from its liganded geometry to its deliganded one.

AB - A time-resolved circular dichroism (CD) experiment is carried out on carbonmonoxy-myoglobin. The CD is measured with a sub-picosecond time resolution after ligand dissociation and the data are interpreted thanks to a classical CD calculation based on the polarizability theory. We observe a decrease of the CD signal in a few picoseconds and a sub-100 ps relaxation towards steady-state deoxy-myoglobin values which we assign to a stress of the proximal histidine which relaxes with the global reorganization of the protein from its liganded geometry to its deliganded one.

U2 - 10.1016/j.cplett.2005.09.022

DO - 10.1016/j.cplett.2005.09.022

M3 - Article

AN - SCOPUS:27644513339

SN - 0009-2614

VL - 415

SP - 313

EP - 316

JO - Chemical Physics Letters

JF - Chemical Physics Letters

IS - 4-6

ER -

Observation of sub-100 ps conformational changes in photolyzed carbonmonoxy-myoglobin probed by time-resolved circular dichroism

Abstract

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