Optical spectroscopic studies of light-harvesting by pigment-reconstituted peridinin-chlorophyll-proteins at cryogenic temperatures.

Optical spectroscopic studies of light-harvesting by pigment-reconstituted peridinin-chlorophyll-proteins at cryogenic temperatures. Research Abstract Details 

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Optical spectroscopic studies of light-harvesting by pigment-reconstituted peridinin-chlorophyll-proteins at cryogenic temperatures. Abstract Text:

Robielyn P Ilagan,Timothy W Chapp,Roger G Hiller,Frank P Sharples, ,Harry A Frank,

Low temperature, steady-state, optical spectroscopic methods were used to study the spectral features of peridinin-chlorophyll-protein (PCP) complexes in which recombinant apoprotein has been refolded in the presence of peridinin and either chlorophyll a (Chl a), chlorophyll b (Chl b), chlorophyll d (Chl d), 3-acetyl-chlorophyll a (3-acetyl-Chl a) or bacteriochlorophyll a (BChl a). Absorption spectra taken at 10 K provide better resolution of the spectroscopic bands than seen at room temperature and reveal specific pigment-protein interactions responsible for the positions of the Qy bands of the chlorophylls. The study reveals that the functional groups attached to Ring I of the two protein-bound chlorophylls modulate the Qy and Soret transition energies. Fluorescence excitation spectra were used to compute energy transfer efficiencies of the various complexes at room temperature and these were correlated with previously reported ultrafast, time-resolved optical spectroscopic dynamics data. The results illustrate the robust nature and value of the PCP complex, which maintains a high efficiency of antenna function even in the presence of non-native chlorophyll species, as an effective tool for elucidating the molecular details of photosynthetic light-harvesting.

Optical spectroscopic studies of light-harvesting by pigment-reconstituted peridinin-chlorophyll-proteins at cryogenic temperatures. Publishing Authors By Initials

RP Ilagan,TW Chapp,RG Hiller,FP Sharples,T ,HA Frank,

For similar investigative techniques: chemistry, analytical: photometry: spectrophotometry research abstracts see: investigative techniques: chemistry, analytical: photometry: spectrophotometry research

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Optical spectroscopic studies of light-harvesting by pigment-reconstituted peridinin-chlorophyll-proteins at cryogenic temperatures. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Photosynthesis research

VOLUME: 90

Page Numbers: 5-15

Journal Abbreviation: Photosyn. Res.

ISSN: 0166-8595

DAY: 3

MONTH: Oct

YEAR: 2006

Optical spectroscopic studies of light-harvesting by pigment-reconstituted peridinin-chlorophyll-proteins at cryogenic temperatures. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 100954728

Optical spectroscopic studies of light-harvesting by pigment-reconstituted peridinin-chlorophyll-proteins at cryogenic temperatures. Keywords Mesh Terms:

KEYWORDS: Spectrophotometry

MESH TERMS: physiology

Chemical & Substance for Abstract: Optical spectroscopic studies of light-harvesting by pigment-reconstituted peridinin-chlorophyll-proteins at cryogenic temperatures. Information

Substance Name: Carotenoids

Registry Number: 36-88-4

Grant and Affiliation Information for Optical spectroscopic studies of light-harvesting by pigment-reconstituted peridinin-chlorophyll-proteins at cryogenic temperatures.

AFFILIATION: Department of Chemistry, University of Connecticut, 55 North Eagleville Road, Storrs, CT 06269-3060 USA.

Country: Netherlands

AGENCY: United States NIGMS

GRANT: GM-30353

ACRONYM: GM

MEDLINETA: Photosynth Res

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