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Participation of bacteriorhodopsin active-site lysine backbone in vibrations associated with retinal photochemistry.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Pinevsky, I. Takei, H. Sigrist, Hans Lewis, Ann Sheves, Mordechai |
| Copyright Year | 1992 |
| Abstract | Bacteriorhodopsin (bR) has been biosynthetically prepared with lysine deuterated at its alpha carbon (C alpha--H). The labeled membranes containing bR were investigated by difference Fourier transform infrared (FTIR) spectroscopy. It has been derived from K/bR and M/bR difference spectra (K and M are photocycle intermediates) that several bands previously assigned to the retinal chromophore are coupled to the C alpha--H. The vibrational modes that exhibit this coupling are principally associated with C15--H and N--H vibrations. [C alpha--2H]Lysine-labeled bR was fragmented enzymatically, and bR structures were regenerated with the C alpha--2H label either on lysine-216 and -172 or on the remaining five lysine residues of the protein. FTIR studies of the regenerated bR system, together with methylation of all lysines except the active-site lysine, reveal that the changes observed due to backbone labeling arise from the active-site lysine. The intensity of the C15--H out-of-plane wag is interpreted as a possible indication of a twist around the C15 = N bond. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://www.pnas.org/content/89/6/2434.full.pdf |
| PubMed reference number | 1549607v1 |
| Volume Number | 89 |
| Issue Number | 6 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Bacteriorhodopsins Bands Lysine PersonNameUse - assigned Photochemistry Retinaldehyde Spectroscopy, Fourier Transform Infrared Spectroscopy, Near-Infrared Tissue membrane Tracer Vertebral column Vibration - physical agent newton |
| Content Type | Text |
| Resource Type | Article |