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The structures of the active center in dark-adapted bacteriorhodopsin by solution-state NMR spectroscopy

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78489

Patzelt,  H.
Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78209

Kessler,  B.
Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78468

Oesterhelt,  D.
Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78477

Oschkinat,  H.
Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Patzelt, H., Simon, B., terLaak, A., Kessler, B., Kuhne, R., Schmieder, P., et al. (2002). The structures of the active center in dark-adapted bacteriorhodopsin by solution-state NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America, 99(15), 9765-9770.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6EB4-9
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 Angstrom 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-C14region, while leaving W182 and T178 essentially unchanged. The N-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-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.