Harald Otto

Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin.

Harald Otto, T Marti, M. Holz et al. · Proceedings of the National Academy of Sciences · 1989 · 319 citations · Full text

Natural Sciences, Biochemistry, Biophysics +13

Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base.

Harald Otto, T Marti, M. Holz et al. · Proceedings of the National Academy of Sciences · 1990 · 233 citations

Life Sciences, Biochemistry, Biophysics +15

Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement.

M. Holz, Toshio Mogi, Harald Otto et al. · Proceedings of the National Academy of Sciences · 1989 · 204 citations · Full text

Natural Sciences, Biochemistry, Biophysics +13

Light-induced Proton Release of Phytochrome Is Coupled to the Transient Deprotonation of the Tetrapyrrole Chromophore

Berthold Borucki, David von Stetten, Sven Seibeck et al. · Journal of Biological Chemistry · 2005 · 169 citations · Full text

Natural Sciences, Biochemistry, Chemistry +17

Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocation.

T Marti, Harald Otto, Toshio Mogi et al. · Journal of Biological Chemistry · 1991 · 114 citations · Full text

Life Sciences, Biochemistry, Biophysics +13