Thermochromism of bacteriorhodopsin and its pH dependence.
Purple membranes (PMs), which consist of the photochromic membrane protein bacteriorhodopsin (BR) and lipids only, show complex thermochromic properties. Three different types of reversible temperature-dependent spectral transitions were found, involving spectral states absorbing at 460, 519, and 630 nm. These thermochromic absorption changes were analyzed in the range from 10 to 80 degrees C. In dependence on the bulk pH value, hypsochromic or bathochromic shifts in the BR absorption spectra are observed in BR gels as well as in BR films. The thermochromic changes between both purple and blue or purple and red were quantified in the CIE color system. The molecular changes causing these effects are discussed, and a model is presented in terms of intramolecular protonation equilibriums. The thermochromic properties of BR may be of interest in applications like security tags, as this feature may complement the well-known photochromic properties of BR.
Neebe
Martin
M
Department of Chemistry, University of Marburg, Hans-Meerwein-Strasse, Marburg, Germany. hampp@staff.uni-marburg.de
Rhinow
Daniel
D
Schromczyk
Nina
N
Hampp
Norbert A
NA
D001436:Bacteriorhodopsins / Q000737:chemistry*; D003124:Colorimetry; D006863:Hydrogen-Ion Concentration; D013056:Spectrophotometry, Ultraviolet
D001436:Bacteriorhodopsins