Comparison of the thermodynamic landscapes of unfolding and formation of the energy dissipative state in the isolated light harvesting complex II.
Comparison of the thermodynamic landscapes of unfolding and formation of the energy dissipative state in the isolated light harvesting complex II.
复制标题
孤立光收集复合体 II 中能量耗散态展开和形成的热力学景观的比较。
DOI:
10.1016/j.bpj.2009.06.005
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发表时间:
2009
影响因子:
3.4
通讯作者:
Santabarbara S
中科院分区:
文献类型:
--
作者:
Santabarbara S
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 (ΔHq= 85 ± 3 kJ mol−1compared to 125 ± 5 kJ mol−1in monomers), which enables the fine-tuning of nonphotochemical quenching in vivo.
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影响因子:
--
作者:
J. M. Beechem
通讯作者:
J. M. Beechem
影响因子:
6.8
作者:
Dobson, Christopher M.;Karplus, Martin
通讯作者:
Karplus, Martin
DOI:
--
发表时间:
1996
期刊:
影响因子:
--
作者:
R. Jennings;R. Bassi;G. Zucchelli
通讯作者:
G. Zucchelli
影响因子:
2.9
作者:
V. Gulbinas;R. Karpicz;G. Garab;L. Valkunas
通讯作者:
L. Valkunas
DOI:
--
发表时间:
1999
期刊:
Biochimica et Biophysica Acta
影响因子:
--
作者:
Santabarbara;Garlaschi;Zucchelli;Jennings
通讯作者:
Jennings