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. 1992 Mar 15;89(6):2434–2438. doi: 10.1073/pnas.89.6.2434

Participation of bacteriorhodopsin active-site lysine backbone in vibrations associated with retinal photochemistry.

Y Gat 1, M Grossjean 1, I Pinevsky 1, H Takei 1, Z Rothman 1, H Sigrist 1, A Lewis 1, M Sheves 1
PMCID: PMC48672  PMID: 1549607

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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