Femtosecond time-resolved absorption spectroscopy of main-form and high-salt peridinin-chlorophyll a-proteins at low temperatures.

Femtosecond time-resolved absorption spectroscopy of main-form and high-salt peridinin-chlorophyll a-proteins at low temperatures. Research Abstract Details 

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Femtosecond time-resolved absorption spectroscopy of main-form and high-salt peridinin-chlorophyll a-proteins at low temperatures. Abstract Text:

Robielyn P Ilagan,Jeremy F Koscielecki,Roger G Hiller,Frank P Sharples,George N Gibson,Robert R Birge,Harry A Frank,

Steady-state and femtosecond time-resolved optical methods have been used to compare the spectroscopic features and energy transfer dynamics of two systematically different light-harvesting complexes from the dinoflagellate Amphidinium carterae: main-form (MFPCP) and high-salt (HSPCP) peridinin-chlorophyll a-proteins. Pigment analysis and X-ray diffraction structure determinations [Hofmann, E., Wrench, P. M., Sharples, F. P., Hiller, R. G., Welte, W., Diederichs, K. (1996) Science 272, 1788-1791; T. Schulte, F. P. Sharples, R. G. Hiller, and E. Hofmann, unpublished results] have revealed the composition and geometric arrangements of the protein-bound chromophores. The MFPCP contains eight peridinins and two chlorophyll (Chl) a, whereas the HSPCP has six peridinins and two Chl a, but both have very similar pigment orientations. Analysis of the absorption spectra has shown that the peridinins and Chls absorb at different wavelengths in the two complexes. Also, in the HSPCP complex, the Qy transitions of the Chls are split into two well-resolved bands. Quantum computations by modified neglect of differential overlap with partial single and double configuration interaction (MNDO-PSDCI) methods have revealed that charged amino acid residues within 8 A of the pigment molecules are responsible for the observed spectral shifts. Femtosecond time-resolved optical spectroscopic kinetic data from both complexes show ultrafast (<130 fs) and slower (approximately 2 ps) pathways for energy transfer from the peridinin excited singlet states to Chl. The Chl-to-Chl energy transfer rate constant for both complexes was measured and is discussed in terms of the Förster mechanism. It was found that, upon direct Chl excitation, the Chl-to-Chl energy transfer rate constant for MFPCP was a factor of 4.2 larger than for HSPCP. It is suggested that this difference arises from a combination of factors including distance between Chls, spectral overlap, and the presence of two additional peridinins in MFPCP that act as polarizable units enhancing the rate of Chl-to-Chl energy transfer. The study has revealed specific pigment-protein interactions that control the spectroscopic features and energy transfer dynamics of these light-harvesting complexes.

Femtosecond time-resolved absorption spectroscopy of main-form and high-salt peridinin-chlorophyll a-proteins at low temperatures. Publishing Authors By Initials

RP Ilagan,JF Koscielecki,RG Hiller,FP Sharples,GN Gibson,RR Birge,HA Frank,

For similar investigative techniques: chemistry, analytical: crystallography: x-ray diffraction research abstracts see: investigative techniques: chemistry, analytical: crystallography: x-ray diffraction research

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Femtosecond time-resolved absorption spectroscopy of main-form and high-salt peridinin-chlorophyll a-proteins at low temperatures. Journal Published:

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

Journal: Biochemistry

VOLUME: 45

Page Numbers: 14052-63

Journal Abbreviation: Biochemistry

ISSN: 0006-2960

DAY: 28

MONTH: Nov

YEAR: 2006

Femtosecond time-resolved absorption spectroscopy of main-form and high-salt peridinin-chlorophyll a-proteins at low temperatures. Information

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LANGUAGE: eng

NlmUniqueID: 370623

Femtosecond time-resolved absorption spectroscopy of main-form and high-salt peridinin-chlorophyll a-proteins at low temperatures. Keywords Mesh Terms:

KEYWORDS: X-Ray Diffraction

MESH TERMS: chemistry

Chemical & Substance for Abstract: Femtosecond time-resolved absorption spectroscopy of main-form and high-salt peridinin-chlorophyll a-proteins at low temperatures. Information

Substance Name: chlorophyll a

Registry Number: 479-61-8

Grant and Affiliation Information for Femtosecond time-resolved absorption spectroscopy of main-form and high-salt peridinin-chlorophyll a-proteins at low temperatures.

AFFILIATION: Department of Chemistry, University of Connecticut, Storrs, Connecticut 06269-3060, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM-34548

ACRONYM: GM

MEDLINETA: Biochemistry

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