AI Article Synopsis
- The study investigates ultrafast infrared transient absorption in the carbonyl region of protonated aspartate and glutamate residues in channelrhodopsin-2, demonstrating an immediate response from the protein when retinal is excited.
- Difference bands appear on a subpicosecond time scale, indicating energy transfer from retinal to nearby side chains, particularly D156 and E90, showcasing strong interactions within the protein.
- The findings suggest that this rapid energy transfer is crucial for the functioning of channelrhodopsin-2 as an optically gated ion channel.
Article 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.
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| http://dx.doi.org/10.1021/acs.jpclett.8b03382 | DOI Listing |
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