Thermally activated superradiance and intersystem crossing in the water-soluble chlorophyll binding protein

T. Renger, Mohamed Madjet, F. Müh, I. Trostmann, F. J. Schmitt, C. Theiss, H. Paulsen, H. J. Eichler, A. Knorr, G. Renger

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

The crystal structure of the class IIb water-soluble chlorophyll binding protein (WSCP) from Lepidium virginicum is used to model linear absorption and circular dichroism spectra as well as excited state decay times of class IIa WSCP from cauliflower reconstituted with chlorophyll (Chl) a and Chl b. The close agreement between theory and experiment suggests that both types of WSCP share a common Chl binding motif, where the opening angle between pigment planes in class IIa WSCP should not differ by more than 10° from that in class IIb. The experimentally observed (Schmitt et al. J. Phys. Chem. B 2008, 112, 13951) decrease in excited state lifetime of Chl a homodimers with increasing temperature is fully explained by thermally activated superradiance via the upper exciton state of the dimer. Whereas a temperature-independent intersystem crossing (ISC) rate is inferred for WSCP containing Chl a homodimers, that of WSCP with Chl b homodimers is found to increase above 100 K. Our quantum chemical/electrostatic calculations suggest that a thermally activated ISC via an excited triplet state T4 is responsible for the latter temperature dependence.

Original languageEnglish
Pages (from-to)9948-9957
Number of pages10
JournalJournal of Physical Chemistry B
Volume113
Issue number29
DOIs
Publication statusPublished - 23 Jul 2009
Externally publishedYes

Fingerprint

Superradiance
Chlorophyll Binding Proteins
chlorophylls
Chlorophyll
proteins
Water
Excited states
water
Pigments
Dimers
Temperature
Carrier Proteins
Electrostatics
Crystal structure
Dichroism
pigments
Excitons
atomic energy levels
dichroism
excitation

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Materials Chemistry
  • Surfaces, Coatings and Films

Cite this

Thermally activated superradiance and intersystem crossing in the water-soluble chlorophyll binding protein. / Renger, T.; Madjet, Mohamed; Müh, F.; Trostmann, I.; Schmitt, F. J.; Theiss, C.; Paulsen, H.; Eichler, H. J.; Knorr, A.; Renger, G.

In: Journal of Physical Chemistry B, Vol. 113, No. 29, 23.07.2009, p. 9948-9957.

Research output: Contribution to journalArticle

Renger, T, Madjet, M, Müh, F, Trostmann, I, Schmitt, FJ, Theiss, C, Paulsen, H, Eichler, HJ, Knorr, A & Renger, G 2009, 'Thermally activated superradiance and intersystem crossing in the water-soluble chlorophyll binding protein', Journal of Physical Chemistry B, vol. 113, no. 29, pp. 9948-9957. https://doi.org/10.1021/jp901886w
Renger, T. ; Madjet, Mohamed ; Müh, F. ; Trostmann, I. ; Schmitt, F. J. ; Theiss, C. ; Paulsen, H. ; Eichler, H. J. ; Knorr, A. ; Renger, G. / Thermally activated superradiance and intersystem crossing in the water-soluble chlorophyll binding protein. In: Journal of Physical Chemistry B. 2009 ; Vol. 113, No. 29. pp. 9948-9957.
@article{ecbba696e43e40158b76973f7bba341e,
title = "Thermally activated superradiance and intersystem crossing in the water-soluble chlorophyll binding protein",
abstract = "The crystal structure of the class IIb water-soluble chlorophyll binding protein (WSCP) from Lepidium virginicum is used to model linear absorption and circular dichroism spectra as well as excited state decay times of class IIa WSCP from cauliflower reconstituted with chlorophyll (Chl) a and Chl b. The close agreement between theory and experiment suggests that both types of WSCP share a common Chl binding motif, where the opening angle between pigment planes in class IIa WSCP should not differ by more than 10° from that in class IIb. The experimentally observed (Schmitt et al. J. Phys. Chem. B 2008, 112, 13951) decrease in excited state lifetime of Chl a homodimers with increasing temperature is fully explained by thermally activated superradiance via the upper exciton state of the dimer. Whereas a temperature-independent intersystem crossing (ISC) rate is inferred for WSCP containing Chl a homodimers, that of WSCP with Chl b homodimers is found to increase above 100 K. Our quantum chemical/electrostatic calculations suggest that a thermally activated ISC via an excited triplet state T4 is responsible for the latter temperature dependence.",
author = "T. Renger and Mohamed Madjet and F. M{\"u}h and I. Trostmann and Schmitt, {F. J.} and C. Theiss and H. Paulsen and Eichler, {H. J.} and A. Knorr and G. Renger",
year = "2009",
month = "7",
day = "23",
doi = "10.1021/jp901886w",
language = "English",
volume = "113",
pages = "9948--9957",
journal = "Journal of Physical Chemistry B Materials",
issn = "1520-6106",
publisher = "American Chemical Society",
number = "29",

}

TY - JOUR

T1 - Thermally activated superradiance and intersystem crossing in the water-soluble chlorophyll binding protein

AU - Renger, T.

AU - Madjet, Mohamed

AU - Müh, F.

AU - Trostmann, I.

AU - Schmitt, F. J.

AU - Theiss, C.

AU - Paulsen, H.

AU - Eichler, H. J.

AU - Knorr, A.

AU - Renger, G.

PY - 2009/7/23

Y1 - 2009/7/23

N2 - The crystal structure of the class IIb water-soluble chlorophyll binding protein (WSCP) from Lepidium virginicum is used to model linear absorption and circular dichroism spectra as well as excited state decay times of class IIa WSCP from cauliflower reconstituted with chlorophyll (Chl) a and Chl b. The close agreement between theory and experiment suggests that both types of WSCP share a common Chl binding motif, where the opening angle between pigment planes in class IIa WSCP should not differ by more than 10° from that in class IIb. The experimentally observed (Schmitt et al. J. Phys. Chem. B 2008, 112, 13951) decrease in excited state lifetime of Chl a homodimers with increasing temperature is fully explained by thermally activated superradiance via the upper exciton state of the dimer. Whereas a temperature-independent intersystem crossing (ISC) rate is inferred for WSCP containing Chl a homodimers, that of WSCP with Chl b homodimers is found to increase above 100 K. Our quantum chemical/electrostatic calculations suggest that a thermally activated ISC via an excited triplet state T4 is responsible for the latter temperature dependence.

AB - The crystal structure of the class IIb water-soluble chlorophyll binding protein (WSCP) from Lepidium virginicum is used to model linear absorption and circular dichroism spectra as well as excited state decay times of class IIa WSCP from cauliflower reconstituted with chlorophyll (Chl) a and Chl b. The close agreement between theory and experiment suggests that both types of WSCP share a common Chl binding motif, where the opening angle between pigment planes in class IIa WSCP should not differ by more than 10° from that in class IIb. The experimentally observed (Schmitt et al. J. Phys. Chem. B 2008, 112, 13951) decrease in excited state lifetime of Chl a homodimers with increasing temperature is fully explained by thermally activated superradiance via the upper exciton state of the dimer. Whereas a temperature-independent intersystem crossing (ISC) rate is inferred for WSCP containing Chl a homodimers, that of WSCP with Chl b homodimers is found to increase above 100 K. Our quantum chemical/electrostatic calculations suggest that a thermally activated ISC via an excited triplet state T4 is responsible for the latter temperature dependence.

UR - http://www.scopus.com/inward/record.url?scp=67650793214&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=67650793214&partnerID=8YFLogxK

U2 - 10.1021/jp901886w

DO - 10.1021/jp901886w

M3 - Article

C2 - 19555085

AN - SCOPUS:67650793214

VL - 113

SP - 9948

EP - 9957

JO - Journal of Physical Chemistry B Materials

JF - Journal of Physical Chemistry B Materials

SN - 1520-6106

IS - 29

ER -