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Article Dans Une Revue Biochimica biophysica acta (BBA) - Bioenergetics Année : 2018

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

Résumé

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.

Dates et versions

hal-02179080 , version 1 (10-07-2019)

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Cristian Ilioaia, Tjaart P. J. Krüger, Oana Ilioaia, Bruno Robert, Rienk Van Grondelle, et al.. Apoprotein heterogeneity increases spectral disorder and a step-wise modification of the B850 fluorescence peak position. Biochimica biophysica acta (BBA) - Bioenergetics, 2018, 1859 (2), pp.137--144. ⟨10.1016/j.bbabio.2017.11.003⟩. ⟨hal-02179080⟩
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