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

Research output: Contribution to JournalArticleAcademicpeer-review

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
DOIs
Publication statusPublished - Feb 2018

Fingerprint

Apoproteins
Fluorescence
Photons
Light
Rhodopseudomonas
Photosynthetic Reaction Center Complex Proteins
Bacteria
Availability
Molecules

Keywords

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

Cite this

Ilioaia, Cristian ; Krüger, Tjaart P.J. ; Ilioaia, Oana ; Robert, Bruno ; van Grondelle, Rienk ; Gall, Andrew. / Apoprotein heterogeneity increases spectral disorder and a step-wise modification of the B850 fluorescence peak position. In: Biochimica et Biophysica Acta - Bioenergetics. 2018 ; Vol. 1859, No. 2. pp. 137-144.
@article{ddb921959b5d4bbc8ee22400969bb40b,
title = "Apoprotein heterogeneity increases spectral disorder and a step-wise modification of the B850 fluorescence peak position",
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.",
keywords = "Light harvesting complexes, Photosynthesis, Purple bacteria, Single molecule spectroscopy",
author = "Cristian Ilioaia and Kr{\"u}ger, {Tjaart P.J.} and Oana Ilioaia and Bruno Robert and {van Grondelle}, Rienk and Andrew Gall",
year = "2018",
month = "2",
doi = "10.1016/j.bbabio.2017.11.003",
language = "English",
volume = "1859",
pages = "137--144",
journal = "Biochimica et Biophysica Acta (BBA) - Bioenergetics",
issn = "0005-2728",
publisher = "Elsevier",
number = "2",

}

Apoprotein heterogeneity increases spectral disorder and a step-wise modification of the B850 fluorescence peak position. / Ilioaia, Cristian; Krüger, Tjaart P.J.; Ilioaia, Oana; Robert, Bruno; van Grondelle, Rienk; Gall, Andrew.

In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 1859, No. 2, 02.2018, p. 137-144.

Research output: Contribution to JournalArticleAcademicpeer-review

TY - JOUR

T1 - Apoprotein heterogeneity increases spectral disorder and a step-wise modification of the B850 fluorescence peak position

AU - Ilioaia, Cristian

AU - Krüger, Tjaart P.J.

AU - Ilioaia, Oana

AU - Robert, Bruno

AU - van Grondelle, Rienk

AU - Gall, Andrew

PY - 2018/2

Y1 - 2018/2

N2 - 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.

AB - 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.

KW - Light harvesting complexes

KW - Photosynthesis

KW - Purple bacteria

KW - Single molecule spectroscopy

UR - http://www.scopus.com/inward/record.url?scp=85035761466&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85035761466&partnerID=8YFLogxK

U2 - 10.1016/j.bbabio.2017.11.003

DO - 10.1016/j.bbabio.2017.11.003

M3 - Article

VL - 1859

SP - 137

EP - 144

JO - Biochimica et Biophysica Acta (BBA) - Bioenergetics

JF - Biochimica et Biophysica Acta (BBA) - Bioenergetics

SN - 0005-2728

IS - 2

ER -