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Unraveling the Intrinsic Color of Chlorophyll

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Rubio,  Angel
Theory Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society;
Nano-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);

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Citation

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.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-B288-A
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.