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

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.

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Genre: Journal Article
Alternative Title : Proc. Natl. Acad. Sci. U. S. A.

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Patzelt, H.1, Author           
Simon, B., Author
terLaak, A., Author
Kessler, B.1, Author           
Kuhne, R., Author
Schmieder, P., Author
Oesterhelt, D.1, Author           
Oschkinat, H.1, Author           
Affiliations:
1Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565164              

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 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.

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Language(s): eng - English
 Dates: 2002-07-23
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41683
ISI: 000177042400032
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Alternative Title : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Affiliations:
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Pages: - Volume / Issue: 99 (15) Sequence Number: - Start / End Page: 9765 - 9770 Identifier: ISSN: 0027-8424