Comparison of the thermodynamic landscapes of unfolding and formation of the energy dissipative state in the isolated light harvesting complex ii

Santabarbara, S. and Horton, P. and Ruban, A.V. (2009) Comparison of the thermodynamic landscapes of unfolding and formation of the energy dissipative state in the isolated light harvesting complex ii. Biophysical Journal, 97 (4). pp. 1188-1197. ISSN 0006-3495 (http://dx.doi.org/10.1016/j.bpj.2009.06.005)

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Abstract

In biochemistry and cell biology, understanding the molecular mechanisms by which physiological processes are regulated is regarded as an ultimate goal. In higher plants, one of the most widely investigated regulatory processes occurs in the light harvesting complexes (LHCII) of the chloroplast thylakoid membranes. Under limiting photon flux densities, LHCII harvests sunlight with high efficiency. When the intensity of incident radiation reaches levels close to the saturation of the photosynthesis, the efficiency of light harvesting is decreased by a process referred to as nonphotochemical quenching (NPQ), which enhances the singlet-excited state deactivation via nonradiative dissipative processes. Conformational rearrangements in LHCII are known to be crucial in promoting and controlling NPQ in vitro and in vivo. In this article, we address the thermodynamic nature of the conformational rearrangements promoting and controlling NPQ in isolated LHCII. A combined, linear reaction scheme in which the folded, quenched state represents a stable intermediate on the unfolding pathway was employed to describe the temperature dependence of the spectroscopic signatures associated with the chlorophyll fluorescence quenching and the loss of secondary structure motifs in LHCII. The thermodynamic model requires considering the temperature dependence of Gibbs free energy difference between the quenched and the unquenched states, as well as the unfolded and quenched states, of LHCII. Even though the same reaction scheme is adequate to describe the quenching and the unfolding processes in LHCII monomers and trimers, their thermodynamic characteristics were found to be markedly different. The results of the thermodynamic analysis shed light on the physiological importance of the trimeric state of LHCII in stabilizing the efficient light harvesting mode as well as preventing the quenched conformation of the protein from unfolding. Moreover, the transition to the quenched conformation in trimers reveals a larger degree of cooperativity than in monomers, explained by a small characteristic entropy (Delta H-q = 85 +/- 3 kJ mol(-1) compared to 125 +/- 5 kJ mol(-1) in monomers), which enables the fine-tuning of nonphotochemical quenching in vivo.

  • Item type:Article
    ID code:19005
    Dates:
    Date
    Event
    19 August 2009
    Published
    Subjects:Science > Physics
    Department:Faculty of Science > Physics
    Depositing user: Strathprints Administrator
    Date deposited:20 May 2010 10:05
    Last modified:08 Apr 2024 17:55
    URI:https://strathprints.strath.ac.uk/id/eprint/19005
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