Ultrafast Protein Response in Channelrhodopsin-2 Studied by Time-Resolved Infrared Spectroscopy.

Autor:	Bühl E; Institute of Physical and Theoretical Chemistry , Goethe University , Max von Laue-Straße 7 , 60438 Frankfurt am Main , Germany., Eberhardt P; Institute of Physical and Theoretical Chemistry , Goethe University , Max von Laue-Straße 7 , 60438 Frankfurt am Main , Germany., Bamann C; Max Planck Institute of Biophysics , Max von Laue-Straße 3 , 60438 Frankfurt am Main , Germany., Bamberg E; Max Planck Institute of Biophysics , Max von Laue-Straße 3 , 60438 Frankfurt am Main , Germany., Braun M; Institute of Physical and Theoretical Chemistry , Goethe University , Max von Laue-Straße 7 , 60438 Frankfurt am Main , Germany., Wachtveitl J; Institute of Physical and Theoretical Chemistry , Goethe University , Max von Laue-Straße 7 , 60438 Frankfurt am Main , Germany.
Jazyk:	angličtina
Zdroj:	The journal of physical chemistry letters [J Phys Chem Lett] 2018 Dec 20; Vol. 9 (24), pp. 7180-7184. Date of Electronic Publication: 2018 Dec 17.
DOI:	10.1021/acs.jpclett.8b03382
Abstrakt:	Ultrafast infrared transient absorption in the carbonyl vibrational region of protonated aspartate and glutamate residues in channelrhodopsin-2 from Chlamydomonas reinhardtii shows immediate protein response to retinal excitation. The observed difference bands are formed directly after the excitation on the subpicosecond time scale and were assigned to side chains in the retinal vicinity, such as D156 and E90. This finding implies an ultrafast and effective energy transfer from the retinal to its environment via hydrogen-bonded networks and reveals extraordinarily strong chromophore-protein coupling and intense interaction within the protein. Relevance to the protein function as an optically gated ion channel is discussed.
Databáze:	MEDLINE
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