The Structures of the Active Center in Dark-adapted Bacteriorhodopsin by Solution-state NMR Spectroscopy

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2002 Jul 18

PMID 12119389

Citations 14

Authors

Heiko Patzelt

Bernd Simon

Antonius terLaak

Brigitte Kessler

Ronald Kuhne

Peter Schmieder

Dieter Oesterhelt

Hartmut Oschkinat

Affiliations

Soon will be listed here.

Abstract

The two forms of bacteriorhodopsin present in the dark-adapted state, containing either all-trans or 13-cis,15-syn retinal, were examined by using solution state NMR, and their structures were determined. Comparison of the all-trans and the 13-cis,15-syn forms shows a shift in position of about 0.25 A within the pocket of the protein. Comparing this to the 13-cis,15-anti chromophore of the catalytic cycle M-intermediate structure, the 13-cis,15-syn form demonstrates a less pronounced up-tilt of the retinal C12[bond]C14 region, while leaving W182 and T178 essentially unchanged. The N[bond]H dipole of the Schiff base orients toward the extracellular side in both forms, however, it reorients toward the intracellular side in the 13-cis,15-anti configuration to form the catalytic M-intermediate. Thus, the change of the N[bond]H dipole is considered primarily responsible for energy storage, conformation changes of the protein, and the deprotonation of the Schiff base. The structural similarity of the all-trans and 13-cis,15-syn forms is taken as strong evidence for the ion dipole dragging model by which proton (hydroxide ion) translocation follows the change of the dipole.

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