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

Yanan Guo, Franziska E. Beyle, Beatrix M. Bold, Hiroshi C. Watanabe, Axel Koslowski, Walter Thiel, Peter Hegemann, Marco Marazzi, Marcus Elstner

Research output: Contribution to journalArticle

22 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)3879-3891
Number of pages13
JournalChemical Science
Volume7
Issue number6
DOIs
Publication statusPublished - 2016

ASJC Scopus subject areas

  • Chemistry(all)

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    Guo, Y., Beyle, F. E., Bold, B. M., Watanabe, H. C., Koslowski, A., Thiel, W., Hegemann, P., Marazzi, M., & Elstner, M. (2016). Active site structure and absorption spectrum of channelrhodopsin-2 wild-type and C128T mutant. Chemical Science, 7(6), 3879-3891. https://doi.org/10.1039/c6sc00468g