Výsledky vyhledávání - "I. Trostmann"

Water soluble chlorophyll binding protein of higher plants: A most suitable model system for basic analyses of pigment–pigment and pigment–protein interactions in chlorophyll protein complexes

Autor: Gernot Renger, I. Trostmann, Franz-Josef Schmitt, Hans Joachim Eichler, Thomas Renger, Harald Paulsen, Jörg Pieper, Christoph Theiss

Publikováno v: Journal of Plant Physiology. 168:1462-1472

This short review paper describes spectroscopic studies on pigment–pigment and pigment–protein interactions of chlorophyll (Chl) a and b bound to the recombinant protein of class IIa water soluble chlorophyll protein (WSCP) from cauliflower. Two

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ea5ef00f45477abfed032b3e890b4e9
https://doi.org/10.1016/j.jplph.2010.12.005

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Excitonic Energy Level Structure and Pigment−Protein Interactions in the Recombinant Water-Soluble Chlorophyll Protein. I. Difference Fluorescence Line-Narrowing

Autor: Arvi Freiberg, Margus Rätsep, I. Trostmann, Jörg Pieper, Gernot Renger, Harald Paulsen

Publikováno v: The Journal of Physical Chemistry B. 115:4042-4052

Difference fluorescence line-narrowing spectroscopy at 4.5 K was employed to investigate electron-phonon and electron-vibrational coupling strengths of the lower exciton level of water-soluble chlorophyll-binding protein (WSCP) from cauliflower recon

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c73e9209fa352fd0801bfc82882663f
https://doi.org/10.1021/jp111455g

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Thermally Activated Superradiance and Intersystem Crossing in the Water-Soluble Chlorophyll Binding Protein

Autor: Harald Paulsen, Andreas Knorr, Thomas Renger, Franz-Josef Schmitt, H. J. Eichler, G. Renger, Mohamed Madjet, Frank Müh, I. Trostmann, C. Theiss

Publikováno v: The Journal of Physical Chemistry B. 113:9948-9957

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45a32dd44cbd194a3c699371cb3dcb2b
https://doi.org/10.1021/jp901886w

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Excited State Dynamics in Recombinant Water-Soluble Chlorophyll Proteins (WSCP) from Cauliflower Investigated by Transient Fluorescence Spectroscopy

Autor: Thomas Renger, Franz-Josef Schmitt, J. Pieper, C. Theiss, J. Fuesers, E. H. Hubrich, G. Renger, H. J. Eichler, Harald Paulsen, I. Trostmann

Publikováno v: The Journal of Physical Chemistry B. 112:13951-13961

The present study describes the fluorescence emission properties of recombinant water-soluble chlorophyll (Chl) protein (WSCP) complexes reconstituted with either Chl a or Chl b alone (Chl a only or Chl b only WSCP, respectively) or mixtures of both

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6bbd724bb05d52bf718aa422dac53bc
https://doi.org/10.1021/jp8024057

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Pigment−Pigment and Pigment−Protein Interactions in Recombinant Water-Soluble Chlorophyll Proteins (WSCP) from Cauliflower

Autor: Thomas Renger, Harald Paulsen, C. Theiss, Andree S, I. Trostmann, H. J. Eichler, Franz-Josef Schmitt, G. Renger

Publikováno v: The Journal of Physical Chemistry B. 111:13325-13335

Plants contain water-soluble chlorophyll-binding proteins (WSCPs) that function neither as antennas nor as components of light-induced electron transfer of photosynthesis but are likely constituents of regulatory protective pathways in particular und

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cb3fe50653e02670084a7444d311d56
https://doi.org/10.1021/jp0723968

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Excitonic energy level structure and pigment-protein interactions in the recombinant water-soluble chlorophyll protein. II. Spectral hole-burning experiments

Autor: Margus Rätsep, Harald Paulsen, Arvi Freiberg, I. Trostmann, Jörg Pieper, Hans Joachim Eichler, Gernot Renger, Christoph Theiss, Franz-Josef Schmitt

Publikováno v: The journal of physical chemistry. B. 115(14)

Persistent spectral hole burning at 4.5 K has been used to investigate the excitonic energy level structure and the excited state dynamics of the recombinant class-IIa water-soluble chlorophyll-binding protein (WSCP) from cauliflower. The hole-burned

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c509a9901a4f415861eec88970c4ba7
https://pubmed.ncbi.nlm.nih.gov/21417356

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Refinement of a structural model of a pigment-protein complex by accurate optical line shape theory and experiments

Autor: G. Renger, Harald Paulsen, and A. Knorr, Thomas Renger, H. J. Eichler, C. Theiss, Mohamed Madjet, I. Trostmann, Marten Richter

Publikováno v: The journal of physical chemistry. B. 111(35)

Time-local and time-nonlocal theories are used in combination with optical spectroscopy to characterize the water-soluble chlorophyll binding protein complex (WSCP) from cauliflower. The recombinant cauliflower WSCP complexes reconstituted with eithe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::987b586163b0f3b9f40ffd48d2c98208
https://pubmed.ncbi.nlm.nih.gov/17696386

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