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Biophys J, August 2002, p. 1136-1146, Vol. 83, No. 2

and
*Department of Chemistry, Graduate School of Science, Kyoto
University, Kyoto 606-8502, Japan, and
Department of Life
Science, Himeji Institute of Technology, Harima Science Garden City,
Kamigori, Akou-gun, Hyogo 678-1297, Japan
Enthalpy changes (
H) of the
photointermediates that appear in the photolysis of octopus rhodopsin
were measured at physiological temperatures by the laser-induced
transient grating method. The enthalpy from the initial state,
rhodopsin, to bathorhodopsin, lumirhodopsin, mesorhodopsin, transient
acid metarhodopsin, and acid metarhodopsin were 146 ± 15 kJ/mol,
122 ± 17 kJ/mol, 38 ± 8 kJ/mol, 12 ± 5 kJ/mol, and
12 ± 5 kJ/mol, respectively. These values, except for
lumirhodopsin, are similar to those obtained for the cryogenically
trapped intermediate species by direct calorimetric measurements.
However, the
H of lumirhodopsin at physiological temperatures is quite different from that at low temperature. The
reaction volume changes of these processes were determined by the
pulsed laser-induced photoacoustic method along with the above
H values. Initially, in the transformation between
rhodopsin and bathorhodopsin, a large volume expansion of +32 ± 3 ml/mol was obtained. The volume changes of the subsequent reaction
steps were rather small. These results are compared with the structural changes of the chromophore, peptide backbone, and water molecules within the membrane helixes reported previously.
Biophys J, August 2002, p. 1136-1146, Vol. 83, No. 2
© 2002 by the Biophysical Society 0006-3495/02/08/1136/11 $2.00
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