Charge Recombination Kinetics and Protein Dynamics in Wild Type and Carotenoid-less Bacterial Reaction Centers: Studies in Trehalose Glasses

详细信息    查看全文

• 作者：Francesco Francia ; Marco Malferrari ; Sophie Sacquin-Mora ; Giovanni Venturoli
• 刊名：Journal of Physical Chemistry B
• 出版年：2009
• 出版时间：July 30, 2009
• 年：2009
• 卷：113
• 期：30
• 页码：10389-10398
• 全文大小：247K
• 年卷期：v.113,no.30(July 30, 2009)
• ISSN：1520-5207

文摘

The coupling between electron transfer and protein dynamics has been investigated in reaction centers (RCs) from the wild type (wt) and the carotenoid-less strain R26 of the photosynthetic bacterium Rhodobacter sphaeroides. Recombination kinetics between the primary photoreduced quinone acceptor (Q_A⁻) and photoxidized donor (P⁺) have been analyzed at room temperature in RCs incorporated into glassy trehalose matrices of different water/sugar ratios. As previously found in R26 RCs, also in the wt RC, upon matrix dehydration, P⁺Q_A⁻ recombination accelerates and becomes broadly distributed, reflecting the inhibition of protein relaxation from the dark-adapted to the light-adapted conformation and the hindrance of interconversion between conformational substates. While in wet trehalose matrices (down to one water per trehalose molecule) P⁺Q_A⁻ recombination kinetics are essentially coincident in wt and R26 RCs, more extensive dehydration leads to two-times faster and more distributed kinetics in the carotenoid-containing RC, indicating a stronger inhibition of the internal protein dynamics in the wt RC. Coarse-grained Brownian dynamics simulations performed on the two RC structures reveal a markedly larger flexibility of the R26 RC, showing that a rigid core of residues, close to the quinone acceptors, is specifically softened in the absence of the carotenoid. These experimental and computational results concur to indicate that removal of the carotenoid molecule has long-range effects on protein dynamics and that the structural/dynamical coupling between the protein and the glassy matrix depends strongly upon the local mechanical properties of the protein interior. The data also suggest that the conformational change stabilizing P⁺Q_A⁻ is localized around the Q_A binding pocket.