Processus photochimiques ultra-rapides: Du laboratoire aux systèmes photoactifs naturels

Monique M. Martin; Pascal Plaza; Pascale Changenet-Barret; Agathe Espagne; Mathilde Mahet; Christian Ley; Fabien Lacombat

Processus photochimiques ultra-rapides: Du laboratoire aux systèmes photoactifs naturels

Translated title of the contribution: Ultrafast photochemical processes: From the lab to natural photoactive systems

Monique M. Martin
, Pascal Plaza
, Pascale Changenet-Barret
, Agathe Espagne
, Mathilde Mahet
, Christian Ley
, Fabien Lacombat

PSL research University & IPSL
Université Paris-Sud 11
Institut Curie

Research output: Contribution to journal › Review article › peer-review

Abstract

The UV-Vis subpicosecond absorption spectroscopy has been used to characterize and probe in real-time the primary photoinduced chemical processes in two photosensory proteins extracted from photomotile micro-organisms. This approach to the structure-function relationship of these photoactive proteins consists in comparing their photophysics to that of their chromophore isolated in solution, in order to evidence the specificity of the natural chromophore-protein complex. It has been shown that the photoisomerisation kinetic and quantum yield of the chromophore of photoactive yellow protein (PYP) are controlled by the properties of the protein nanospace in which it is embedded, and also that the oxyblepharism binding protein (OBIP) undergoes photoinduced picosecond reactions.

Translated title of the contribution	Ultrafast photochemical processes: From the lab to natural photoactive systems
Original language	French
Pages (from-to)	14-19
Number of pages	6
Journal	Actualite Chimique
Issue number	320-321
Publication status	Published - 1 Jan 2008

Cite this

@article{a31f554318174c099980762d878b96ad,

title = "Processus photochimiques ultra-rapides: Du laboratoire aux syst{\`e}mes photoactifs naturels",

abstract = "The UV-Vis subpicosecond absorption spectroscopy has been used to characterize and probe in real-time the primary photoinduced chemical processes in two photosensory proteins extracted from photomotile micro-organisms. This approach to the structure-function relationship of these photoactive proteins consists in comparing their photophysics to that of their chromophore isolated in solution, in order to evidence the specificity of the natural chromophore-protein complex. It has been shown that the photoisomerisation kinetic and quantum yield of the chromophore of photoactive yellow protein (PYP) are controlled by the properties of the protein nanospace in which it is embedded, and also that the oxyblepharism binding protein (OBIP) undergoes photoinduced picosecond reactions.",

keywords = "Electron transfer, Photoactive proteins, Photoisomerisation, Photomovement, Subpicosecond spectroscopy",

author = "Martin, \{Monique M.\} and Pascal Plaza and Pascale Changenet-Barret and Agathe Espagne and Mathilde Mahet and Christian Ley and Fabien Lacombat",

year = "2008",

month = jan,

day = "1",

language = "Fran{\c c}ais",

pages = "14--19",

journal = "Actualite Chimique",

issn = "0151-9093",

number = "320-321",

}

TY - JOUR

T1 - Processus photochimiques ultra-rapides

T2 - Du laboratoire aux systèmes photoactifs naturels

AU - Martin, Monique M.

AU - Plaza, Pascal

AU - Changenet-Barret, Pascale

AU - Espagne, Agathe

AU - Mahet, Mathilde

AU - Ley, Christian

AU - Lacombat, Fabien

PY - 2008/1/1

Y1 - 2008/1/1

N2 - The UV-Vis subpicosecond absorption spectroscopy has been used to characterize and probe in real-time the primary photoinduced chemical processes in two photosensory proteins extracted from photomotile micro-organisms. This approach to the structure-function relationship of these photoactive proteins consists in comparing their photophysics to that of their chromophore isolated in solution, in order to evidence the specificity of the natural chromophore-protein complex. It has been shown that the photoisomerisation kinetic and quantum yield of the chromophore of photoactive yellow protein (PYP) are controlled by the properties of the protein nanospace in which it is embedded, and also that the oxyblepharism binding protein (OBIP) undergoes photoinduced picosecond reactions.

AB - The UV-Vis subpicosecond absorption spectroscopy has been used to characterize and probe in real-time the primary photoinduced chemical processes in two photosensory proteins extracted from photomotile micro-organisms. This approach to the structure-function relationship of these photoactive proteins consists in comparing their photophysics to that of their chromophore isolated in solution, in order to evidence the specificity of the natural chromophore-protein complex. It has been shown that the photoisomerisation kinetic and quantum yield of the chromophore of photoactive yellow protein (PYP) are controlled by the properties of the protein nanospace in which it is embedded, and also that the oxyblepharism binding protein (OBIP) undergoes photoinduced picosecond reactions.

KW - Electron transfer

KW - Photoactive proteins

KW - Photoisomerisation

KW - Photomovement

KW - Subpicosecond spectroscopy

M3 - Article de révision

AN - SCOPUS:48649089855

SN - 0151-9093

SP - 14

EP - 19

JO - Actualite Chimique

JF - Actualite Chimique

IS - 320-321

ER -

Processus photochimiques ultra-rapides: Du laboratoire aux systèmes photoactifs naturels

Abstract

Fingerprint

Cite this