Ultrafast Protein Response in Channelrhodopsin-2 Studied by Time-Resolved Infrared Spectroscopy
Elena Bühl1, Peter Eberhardt1, Christian Bamann2
1Institute of Physical and Theoretical Chemistry , Goethe University , Max von Laue-Straße 7 , 60438 Frankfurt am Main , Germany.
Abstract:
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.
Related Concept Videos
Infrared (IR) Spectroscopy: Overview
Different compounds display unique properties due to their...
Attenuated Total Reflectance (ATR) Infrared Spectroscopy: Overview
The ATR process begins by directing a beam...
The Unfolded Protein Response
Regulation of the Unfolded Protein Response
meta-Directing Deactivators: –NO2, –CN, –CHO, –⁠CO2R, –COR, –CO2H
Humoral Immune Responses


