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Unraveling the Electronic Structure of Individual Photosynthetic Pigment-Protein Complexes

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van Oijen, Antoine M., Ketelaars, Martijn, Köhler, Jürgen, Aartsma, Thijs J., Schmidt, Jan·1999·Science

Abstract

Low-temperature single-molecule spectroscopic techniques were applied to a light-harvesting pigment-protein complex (LH2) from purple photosynthetic bacteria. The properties of the electronically excited states of the two circular assemblies (B800 and B850) of bacteriochlorophyll a (BChl a) pigment molecules in the individual complexes were revealed, without ensemble averaging. The results show that the excited states of the B800 ring of pigments are mainly localized on individual BChl a molecules. In contrast, the absorption of a photon by the B850 ring can be consistently described in terms of an excitation that is completely delocalized over the ring. This property may contribute to the high efficiency of energy transfer in these photosynthetic complexes.

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Metadata

Authors
van Oijen, A. M., Ketelaars, M., Köhler, J., Aartsma, T. J., & Schmidt, J.
Venue
Science
Published
1999-07-16
Volume
285
Issue
5426
Pages
400-402
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2102054882
Cited by
530
References
0
FWCI
20.21
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Unraveling the Electronic Structure of Individual Photosynthetic Pigment-Protein Complexes. https://app.cochat.ai/papers/10.1126/science.285.5426.400
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van Oijen, A. M., Ketelaars, M., Köhler, J., Aartsma, T. J., & Schmidt, J. (1999). Unraveling the Electronic Structure of Individual Photosynthetic Pigment-Protein Complexes. Science. https://doi.org/10.1126/science.285.5426.400

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.