Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin

Hans Jürgen Sass, Georg Büldt, Ralf Gessenich, Dominic Hehn, Dirk Neff, Ramona Schlesinger, Joel Berendzen, P. Ormos

Research output: Contribution to journalArticle

297 Citations (Scopus)

Abstract

The transport of protons across membranes is an important process in cellular bioenergetics. The light-driven proton pump bacteriorhodopsin is the best-characterized protein providing this function. Photon energy is absorbed by the chromophore retinal, covalently bound to Lys 216 via a protonated Schiff base. The light-induced all-trans to 13-cis isomerization of the retinal results in deprotonation of the Schiff base followed by alterations in protonatable groups within bacteriorhodopsin. The changed force field induces changes, even in the tertiary structure, which are necessary for proton pumping. The recent report of a high-resolution X-ray crystal structure for the late M intermediate of a mutant bacteriorhopsin (with Asp 96→Asn) displays the structure of a proton pathway highly disturbed by the mutation. To observe an unperturbed proton pathway, we determined the structure of the late M intermediate of wild-type bacteriorhodopsin (2.25 Å resolution). The cytoplasmic side of our M2 structure shows a water net that allows proton transfer from the proton donor group Asp 96 towards the Schiff base. An enlarged cavity system above Asp 96 is observed, which facilitates the de- and reprotonation of this group by fluctuating water molecules in the last part of the cycle.

Original languageEnglish
Pages (from-to)649-653
Number of pages5
JournalNature
Volume406
Issue number6796
DOIs
Publication statusPublished - Aug 10 2000

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Bacteriorhodopsins
Protons
Schiff Bases
Light
Proton Pumps
Water
Viperidae
Photons
Energy Metabolism
X-Rays
Mutation
Membranes
Proteins

ASJC Scopus subject areas

  • General

Cite this

Sass, H. J., Büldt, G., Gessenich, R., Hehn, D., Neff, D., Schlesinger, R., ... Ormos, P. (2000). Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin. Nature, 406(6796), 649-653. https://doi.org/10.1038/35020607

Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin. / Sass, Hans Jürgen; Büldt, Georg; Gessenich, Ralf; Hehn, Dominic; Neff, Dirk; Schlesinger, Ramona; Berendzen, Joel; Ormos, P.

In: Nature, Vol. 406, No. 6796, 10.08.2000, p. 649-653.

Research output: Contribution to journalArticle

Sass, HJ, Büldt, G, Gessenich, R, Hehn, D, Neff, D, Schlesinger, R, Berendzen, J & Ormos, P 2000, 'Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin', Nature, vol. 406, no. 6796, pp. 649-653. https://doi.org/10.1038/35020607
Sass HJ, Büldt G, Gessenich R, Hehn D, Neff D, Schlesinger R et al. Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin. Nature. 2000 Aug 10;406(6796):649-653. https://doi.org/10.1038/35020607
Sass, Hans Jürgen ; Büldt, Georg ; Gessenich, Ralf ; Hehn, Dominic ; Neff, Dirk ; Schlesinger, Ramona ; Berendzen, Joel ; Ormos, P. / Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin. In: Nature. 2000 ; Vol. 406, No. 6796. pp. 649-653.
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