help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Groot, M.-L.
Right arrow Articles by Dekker, J. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Groot, M.-L.
Right arrow Articles by Dekker, J. P.

Biophys J, December 1999, p. 3328-3340, Vol. 77, No. 6

Spectroscopic Properties of the CP43 Core Antenna Protein of Photosystem II

Marie-Louise Groot, Raoul N. Frese, Frank L. de Weerd, Krystyna Bromek, Åsa Pettersson, Erwin J. G. Peterman, Ivo H. M. van Stokkum, Rienk van Grondelle, and Jan P. Dekker

Division of Physics and Astronomy, Institute of Molecular Biological Sciences, Vrije Universiteit, 1081 HV Amsterdam, the Netherlands

CP43 is a chlorophyll-protein complex that funnels excitation energy from the main light-harvesting system of photosystem II to the photochemical reaction center. We purified CP43 from spinach photosystem II membranes in the presence of the nonionic detergent n-dodecyl-beta ,D-maltoside and recorded its spectroscopic properties at various temperatures between 4 and 293 K by a number of polarized absorption and fluorescence techniques, fluorescence line narrowing, and Stark spectroscopy. The results indicate two "red" states in the Qy absorption region of the chlorophylls. The first peaks at 682.5 nm at 4 K, has an extremely narrow bandwidth with a full width at half-maximum of ~2.7 nm (58 cm-1) at 4 K, and has the oscillator strength of a single chlorophyll. The second peaks at ~679 nm, has a much broader bandshape, is caused by several excitonically interacting chlorophylls, and is responsible for all 4 K absorption at wavelengths longer than 685 nm. The Stark spectrum of CP43 resembles the first derivative of the absorption spectrum and has an exceptionally small overall size, which we attribute to opposing orientations of the monomer dipole moments of the excitonically coupled pigments.

Biophys J, December 1999, p. 3328-3340, Vol. 77, No. 6
© 1999 by the Biophysical Society   0006-3495/99/12/3328/13  $2.00


This article has been cited by other articles:


Home page
 Am. J. Bot.Home page
L. Ferroni, C. Baldisserotto, L. Pantaleoni, P. Billi, M. P. Fasulo, and S. Pancaldi
High salinity alters chloroplast morpho-physiology in a freshwater Kirchneriella species (Selenastraceae) from Ethiopian Lake Awasa
Am. J. Botany, December 1, 2007; 94(12): 1972 - 1983.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
N. P. Pawlowicz, M.-L. Groot, I. H. M. van Stokkum, J. Breton, and R. van Grondelle
Charge Separation and Energy Transfer in the Photosystem II Core Complex Studied by Femtosecond Midinfrared Spectroscopy
Biophys. J., October 15, 2007; 93(8): 2732 - 2742.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
G. Zucchelli, D. Brogioli, A. P. Casazza, F. M. Garlaschi, and R. C. Jennings
Chlorophyll Ring Deformation Modulates Qy Electronic Energy in Chlorophyll-Protein Complexes and Generates Spectral Forms
Biophys. J., September 15, 2007; 93(6): 2240 - 2254.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1999 by the Biophysical Society.