Interaction of Asn105 with the retinal chromophore during photoisomerization of pharaonis phoborhodopsin

Biochemistry
Hideki KandoriNaoki Kamo

Abstract

pharaonis phoborhodopsin (ppR; also called pharaonis sensory rhodopsin II, psR-II) is a photoreceptor for negative phototaxis in Natronobacterium pharaonis. ppR has a blue-shifted absorption spectrum with a spectral shoulder, which is highly unique for the archaeal rhodopsin family. The primary reaction of ppR is a cis-trans photoisomerization of the retinal chromophore to form the K intermediate, like the well-studied proton pump bacteriorhodopsin (BR). Recent comparative FTIR spectroscopy of the K states in ppR and BR revealed that more extended structural changes take place in ppR than in BR with respect to chromophore distortion and protein structural changes [Kandori, H., Shimono, K., Sudo, Y., Iwamoto, M., Shichida, Y., and Kamo, N. (2001) Biochemistry 40, 9238-9246]. FTIR spectroscopy of the N105D mutant protein reported here assigns the vibrational bands at 1704 and 1700 cm(-1) as C=O stretches of Asn105 in ppR and ppR(K), respectively. A comparative investigation between ppR and BR further reveals that the structure at position 105 in ppR is similar to that of the corresponding position (Asp115) in BR; this observation is supported by the recent X-ray crystallographic structures of ppR [Luecke, H., Schobert, B., Lanyi,...Continue Reading

Citations

Aug 7, 2002·Current Opinion in Structural Biology·John L Spudich, Hartmut Luecke
Jan 1, 2009·Sensors·Akira Kawanabe, Hideki Kandori
Mar 28, 2007·The Journal of Biological Chemistry·Yuki SudoHideki Kandori
Mar 24, 2020·Chemical Reviews·Victor A Lorenz-Fonfria

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