ArticleBiophysical journal2002
Role of Asp193 in chromophore-protein interaction of pharaonis phoborhodopsin (sensory rhodopsin II).
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Phototactic and chemotactic signal transduction by transmembrane receptors and transducers in microorganisms.Sensors (Basel, Switzerland) · 2010Review
- A long-lived M-like state of phoborhodopsin that mimics the active state.Biophysical journal · 2008Article
- Correlation of the O-intermediate rate with the pKa of Asp-75 in the dark, the counterion of the Schiff base of Pharaonis phoborhodopsin (sensory rhodopsin II).Biophysical journal · 2005Article
- Role of Arg-72 of pharaonis Phoborhodopsin (sensory rhodopsin II) on its photochemistry.Biophysical journal · 2004Article
- Time-resolved FTIR studies of sensory rhodopsin II (NpSRII) from Natronobacterium pharaonis: implications for proton transport and receptor activation.Biophysical journal · 2003Article
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6 authors.
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Abstract
Pharaonis phoborhodopsin (ppR; also pharaonis sensory rhodopsin II, psRII) is a receptor of the negative phototaxis of Natronobacterium pharaonis. By spectroscopic titration of D193N and D193E mutants, the pK(a) of the Schiff base was evaluated. Asp193 corresponds to Glu204 of bacteriorhodopsin (bR). The pK(a) of the Schiff base (SBH(+)) of D193N was approximately 10.1-10.0 (at XH(+)) and approximately 11.4-11.6 (at X) depending on the protonation state of a certain residue (designated by X) and independent of Cl(-), whereas those of the wild type and D193E were >12. The pK(a) values of XH(+) were approximately 11.8-11.2 at the state of SB, 10.5 at SBH(+) state in the presence of Cl(-), and 9.6 at SBH(+) without Cl(-). These imply the presence of a long-range interaction in the extracellular channel. Asp193 was suggested to be deprotonated in the present dodecyl-maltoside (DDM) solubilized wild-type ppR, which is contrary to Glu204 of bR. In the absence of salts, the irreversible denaturation of D193N (but not the wild type and D193E) occurred via a metastable state, into which the addition of Cl(-) reversed the intact pigment. This suggests that the negative charge at residue 193, which can be substituted by Cl(-), is necessary to maintain the proper conformation in the DDM-solubilized ppR.
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