Single and multi-exciton dynamics in aqueous protochlorophyllide aggregates

O. Sytina; I.H.M. van Stokkum; R. van Grondelle; M.L. Groot

doi:10.1021/jp108317u

Single and multi-exciton dynamics in aqueous protochlorophyllide aggregates

O. Sytina, I.H.M. van Stokkum, R. van Grondelle, M.L. Groot

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

In plants, the oxidoreductase enzyme POR reduces protochlorophyllide (Pchlide) into chlorophyllide (Chlide), using NADPH as a cofactor. The reduction involves the transfer of two electrons and two protons to the C17î - C18 double bond of Pchlide, and the reaction is initiated by the absorption of light by Pchlide itself. In this work we have studied the excited state dynamics of Pchlide dissolved in water, where it forms excitonically coupled aggregates, by ultrafast time-resolved transient absorption and fluorescence experiments performed in the 480 - 720 nm visible region and in the 1780 - 1590 cm

Original language	English
Pages (from-to)	3936-3946
Number of pages	11
Journal	Journal of Physical Chemistry A
Volume	115
Issue number	16
DOIs	https://doi.org/10.1021/jp108317u
Publication status	Published - 2011

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title = "Single and multi-exciton dynamics in aqueous protochlorophyllide aggregates",

abstract = "In plants, the oxidoreductase enzyme POR reduces protochlorophyllide (Pchlide) into chlorophyllide (Chlide), using NADPH as a cofactor. The reduction involves the transfer of two electrons and two protons to the C17{\^i} - C18 double bond of Pchlide, and the reaction is initiated by the absorption of light by Pchlide itself. In this work we have studied the excited state dynamics of Pchlide dissolved in water, where it forms excitonically coupled aggregates, by ultrafast time-resolved transient absorption and fluorescence experiments performed in the 480 - 720 nm visible region and in the 1780 - 1590 cm",

author = "O. Sytina and {van Stokkum}, I.H.M. and {van Grondelle}, R. and M.L. Groot",

year = "2011",

doi = "10.1021/jp108317u",

language = "English",

volume = "115",

pages = "3936--3946",

journal = "Journal of Physical Chemistry A",

issn = "1089-5639",

publisher = "American Chemical Society",

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TY - JOUR

T1 - Single and multi-exciton dynamics in aqueous protochlorophyllide aggregates

AU - Sytina, O.

AU - van Stokkum, I.H.M.

AU - van Grondelle, R.

AU - Groot, M.L.

PY - 2011

Y1 - 2011

N2 - In plants, the oxidoreductase enzyme POR reduces protochlorophyllide (Pchlide) into chlorophyllide (Chlide), using NADPH as a cofactor. The reduction involves the transfer of two electrons and two protons to the C17î - C18 double bond of Pchlide, and the reaction is initiated by the absorption of light by Pchlide itself. In this work we have studied the excited state dynamics of Pchlide dissolved in water, where it forms excitonically coupled aggregates, by ultrafast time-resolved transient absorption and fluorescence experiments performed in the 480 - 720 nm visible region and in the 1780 - 1590 cm

AB - In plants, the oxidoreductase enzyme POR reduces protochlorophyllide (Pchlide) into chlorophyllide (Chlide), using NADPH as a cofactor. The reduction involves the transfer of two electrons and two protons to the C17î - C18 double bond of Pchlide, and the reaction is initiated by the absorption of light by Pchlide itself. In this work we have studied the excited state dynamics of Pchlide dissolved in water, where it forms excitonically coupled aggregates, by ultrafast time-resolved transient absorption and fluorescence experiments performed in the 480 - 720 nm visible region and in the 1780 - 1590 cm

U2 - 10.1021/jp108317u

DO - 10.1021/jp108317u

M3 - Article

SN - 1089-5639

VL - 115

SP - 3936

EP - 3946

JO - Journal of Physical Chemistry A

JF - Journal of Physical Chemistry A

IS - 16

ER -

Single and multi-exciton dynamics in aqueous protochlorophyllide aggregates

Abstract

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