Unraveling the intrinsic color of chlorophyll

Bruce F. Milne, Yoni Toker, Angel Rubio, Steen Brøndsted Nielsen

Research output: Contribution to journalArticlepeer-review

52 Scopus citations

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 Chlcontaining 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.

Original languageEnglish
Pages (from-to)2170-2173
Number of pages4
JournalAngewandte Chemie - International Edition
Volume54
Issue number7
DOIs
StatePublished - 9 Feb 2015

Bibliographical note

Publisher Copyright:
© 2015 Wiley-VCH Verlag GmbH & Co. KGaA.

Funding

FundersFunder number
European CommissionFP7 CRONOS 280879-2
European Research CouncilERC-2010-AdG-267374, FIS2013-46159-C3-1-P
Seventh Framework Programme267374, 280879

    Keywords

    • Action spectroscopy
    • Chlorophyll
    • Color tuning
    • Photosynthesis
    • Time-dependent density functional theory

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