Apoprotein heterogeneity increases spectral disorder and a step-wise modification of the B850 fluorescence peak position

Cristian Ilioaia*, Tjaart P.J. Krüger, Oana Ilioaia, Bruno Robert, Rienk van Grondelle, Andrew Gall

*Corresponding author for this work

Research output: Contribution to JournalArticleAcademicpeer-review

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Abstract

It has already been established that the quaternary structure of the main light-harvesting complex (LH2) from the photosynthetic bacterium Rhodopseudomonas palustris is a nonameric ‘ring’ of PucAB heterodimers and under low-light culturing conditions an increased diversity of PucB synthesis occurs. In this work, single molecule fluorescence emission studies show that different classes of LH2 ‘rings’ are present in “low-light” adapted cells and that an unknown chaperon process creates multiple sub-types of ‘rings’ with more conformational sub-states and configurations. This increase in spectral disorder significantly augments the cross-section for photon absorption and subsequent energy flow to the reaction centre trap when photon availability is a limiting factor. This work highlights yet another variant used by phototrophs to gather energy for cellular development.

Original languageEnglish
Pages (from-to)137-144
Number of pages8
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1859
Issue number2
Early online date21 Nov 2017
DOIs
Publication statusPublished - Feb 2018

Keywords

  • Light harvesting complexes
  • Photosynthesis
  • Purple bacteria
  • Single molecule spectroscopy

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