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Active site structure and absorption spectrum of channelrhodopsin-2 wild-type and C128T mutant

MPS-Authors
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Koslowski,  Axel
Research Department Thiel, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Thiel,  W.
Research Department Thiel, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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(Supplementary material), 41MB

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(Supplementary material), 6MB

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(Supplementary material), 7MB

Citation

Guo, Y., Beyle, F. E., Bold, B. M., Watanabe, H. C., Koslowski, A., Thiel, W., et al. (2016). Active site structure and absorption spectrum of channelrhodopsin-2 wild-type and C128T mutant. Chemical Science, 7(6), 3879-3891. doi: 10.1039/C6SC00468G.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002A-E2D1-4
Abstract
In spite of considerable interest, the active site of channelrhodopsin still lacks a detailed atomistic description, the understanding of which could strongly enhance the development of novel optogenetics tools. We present a computational study combining different state-of-the-art techniques, including hybrid quantum mechanics/molecular mechanics schemes and high-level quantum chemical methods, to properly describe the hydrogen-bonding pattern between the retinal chromophore and its counterions in channelrhodopsin-2 Wild-Type and C128T mutant. Especially, we show by extensive ground state dynamics that the active site, containing a glutamic acid (E123) and a water molecule, is highly dynamic, sampling three different hydrogen-bonding patterns. This results in a broad absorption spectrum that is representative of the different structural motifs found. A comparison with bacteriorhodopsin, characterized by a pentagonal hydrogen-bonded active site structure, elucidates their different absorption properties.