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  Unraveling the Intrinsic Color of Chlorophyll

Milne, B. F., Toker, Y., Rubio, A., & Nielsen, S. B. (2015). Unraveling the Intrinsic Color of Chlorophyll. Angewandte Chemie International Edition, 54(7), 2170-2173. doi:10.1002/anie.201410899.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-B288-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0026-A505-D
Genre: Journal Article

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http://dx.doi.org/10.1002/anie.201410899 (Publisher version)
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 Creators:
Milne, Bruce F.1, 2, Author
Toker, Yoni3, Author
Rubio, Angel1, 4, Author              
Nielsen, Steen Brøndsted5, Author
Affiliations:
1Nano-Bio Spectroscopy group and ETSF Scientific Development Centre, Department of Materials Physics, University of the Basque Country, CFM CSIC-UPV/EHU-MPC and DIPC, Avenida de Tolosa 72, E-20018 Donostia (Spain), ou_persistent22              
2Centre for Computational Physics, Department of Physics, University of Coimbra, Rua Larga, 3004-516 Coimbra (Portugal), ou_persistent22              
3Institute of Nanotechnology and Advanced Materials, Bar-Ilan University, Ramat-Gan 5290002 (Israel), ou_persistent22              
4Theory Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_2074320              
5Department of Physics and Astronomy, Aarhus University, Ny Munkegade, DK-8000 Aarhus C (Denmark), ou_persistent22              

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Free keywords: action spectroscopy, chlorophyll, color tuning, photosynthesis, time-dependent density functional theory
 Abstract: The exact color of light absorbed by chlorophyll (Chl) pigments, the light-harvesters in photosynthesis, is tuned by the protein microenvironment, but without knowledge of the intrinsic color of Chl it remains unclear how large this effect is. Experimental first absorption energies of Chl a and b isolated in vacuo and tagged with quaternary ammonium cations are reported. The energies are largely insensitive to details of the tag structure, a finding supported by first-principles calculations using time-dependent density functional theory. Absorption is significantly blue-shifted compared to that of Chl-containing proteins (by 30–70 nm). A single red-shifting perturbation, such as axial ligation or the protein medium, is insufficient to account even for the smallest shift; the largest requires pigment–pigment interactions.

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Language(s): eng - English
 Dates: 2014-11-112014-12-302015-02-09
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201410899
BibTex Citekey: ANIE:ANIE201410899
 Degree: -

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Title: Angewandte Chemie International Edition
  Abbreviation : Angew. Chem. Int. Ed.
Source Genre: Journal
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Publ. Info: Weinheim : Wiley-VCH Verlag GmbH & Co. KGaA
Pages: - Volume / Issue: 54 (7) Sequence Number: - Start / End Page: 2170 - 2173 Identifier: Other: 1521-3773
CoNE: /journals/resource/0570-0833