Previous mutagenesis studies with bacteriorhodopsin have shown that reprotonation of the
Schiff's base is the rate-limiting step in the photocycle of the D96N mutant, whereas retinal re …

Structural intermediates occurring in the photocycle of wild-type bacteriorhodopsin are
trapped by illuminating hydrated, glucose-embedded purple membrane at 170K, 220K …

In the last step of the bacteriorhodopsin photocycle the initial state is regenerated from the O
intermediate in an essentially unidirectional reaction. Comparison of the rate of this …

The structure of an early M-intermediate of the wild-type bacteriorhodopsin photocycle
formed by actinic illumination at 230K has been determined by x-ray crystallography to a …

By varying the pH, the D85N mutant of bacteriorhodopsin provides models for several
photocycle intermediates of the wild-type protein in which D85 is protonated. At pH 10.8 …

We report a comprehensive electron crystallographic analysis of conformational changes in
the photocycle of wild-type bacteriorhodopsin and in a variety of mutant proteins with kinetic …

We report that the replacement of Leu-93 in bacteriorhodopsin by Ala (L93A) or Thr (L93T)
slows down the photocycle by approximately 100-fold relative to wild-type …

During the extended lifetime of the O-state in bacteriorhodopsin (bR) mutant L93A, two
substates have been distinguished. The first O-intermediate (OI) is in rapid equilibrium with …

We previously have presented evidence for prominent structural changes in helices F and G
of bacteriorhodopsin during the photocycle. These changes were determined by carrying out …

We measured time-resolved difference spectra, in the visible and the infrared, for the Glu-
194 and Glu-204 mutants of bacteriorhodopsin and detected an anomalous O state, labeled …