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Biophys J, December 2002, p. 3490-3498, Vol. 83, No. 6

*Max-Planck-Institut für Molekulare Physiologie, 44227 Dortmund, Germany; and
University of Dortmund, Department
of Chemistry, 44227 Dortmund, Germany
The pressure dependence of the photocycle kinetics of
bacteriorhodopsin from Halobacterium salinarium was
investigated at pressures up to 4 kbar at 25°C and 40°C. The
kinetics can be adequately modeled by nine apparent rate constants,
which are assigned to irreversible transitions of a single relaxation
chain of nine kinetically distinguishable states
P1 to P9. All
states except P1 and
P9 consist of two or more spectral
components. The kinetic states P2 to
P6 comprise only the two fast equilibrating
spectral states L and M. From the pressure dependence,
the volume differences
V
V
11.4 ± 0.7 ml/mol
(P2) to
V
V
Biophys J, December 2002, p. 3490-3498, Vol. 83, No. 6
© 2002 by the Biophysical Society 0006-3495/02/12/3490/09 $2.00
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