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Biophys J, February 2000, p. 967-976, Vol. 78, No. 2
and
*Max-Planck-Institut für Molekulare Physiologie,
D-44227 Dortmund, Germany; and Max-Planck-Institut
für Biophysik, D-60596 Frankfurt/Main, Germany
In the present work the light-activated proton transfer
reactions of sensory rhodopsin II from Natronobacterium
pharaonis (pSRII) and those of the channel-mutants D75N-pSRII
and F86D-pSRII are investigated using flash photolysis and black lipid
membrane (BLM) techniques. Whereas the photocycle of the F86D-pSRII
mutant is quite similar to that of the wild-type protein, the
photocycle of D75N-pSRII consists of only two intermediates. The
addition of external proton donors such as azide, or in the case of
F86D-pSRII, imidazole, accelerates the reprotonation of the Schiff
base, but not the turnover. The electrical measurements prove that
pSRII and F86D-pSRII can function as outwardly directed proton pumps, whereas the mutation in the extracellular channel (D75N-pSRII) leads to
an inwardly directed transient current. The almost negligible size of
the photostationary current is explained by the long-lasting photocycle
of about a second. Although the M decay, but not the photocycle
turnover, of pSRII and F86D-pSRII is accelerated by the addition of
azide, the photostationary current is considerably increased. It is
discussed that in a two-photon process a late intermediate (N- and/or
O-like species) is photoconverted back to the original resting state;
thereby the long photocycle is cut short, giving rise to the large
increase of the photostationary current. The results presented in this
work indicate that the function to generate ion gradients across
membranes is a general property of archaeal rhodopsins.
Biophys J, February 2000, p. 967-976, Vol. 78, No. 2
© 2000 by the Biophysical Society 0006-3495/00/02/967/10 $2.00
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