Abstract
The lifetime of the M-state of bacteriorhodopsin (BR) is increased by genetic and chemical modifications and by solubilizing purple membranes (PMs) with detergent. Chemically modified D96E films as well as D96N films, possess close to 100% bleaching efficiency which makes them attractive for use as image storage media. The mutant S35C has spectral and kinetic properties identical to the WT, both in aqueous suspensions and in films. This indicates that substitution of Ser-35 with Cys has an insignificant effect on the photocycling activity of BR. This substitution provides an attachment site that does not interfere with the function of BR. The magnitude of photocurrent transients generated by mutant BR proteins is used to measure the efficiency of the ground-to-M-state transitions.
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