Chromophore Distortions in Photointermediates of Proteorhodopsin visualized by DNP-enhanced solid-state NMR.
J Am Chem Soc. 2017 Oct 13;:
Authors: Mehler M, Eckert CE, Leeder AJ, Kaur J, Fischer T, Kubatova N, Brown LJ, Brown RCD, Becker-Baldus J, Wachtveitl J, Glaubitz C
Abstract
Proteorhodopsin (PR) is the most abundant retinal protein on earth and functions as a light-driven proton pump. Despite of extensive efforts, structural data for PR photointermediate states have not been obtained. Based on DNP-enhanced solid-state NMR, we were able to analyze the retinal polyene chain between positions C10 and C15 as well as the Schiff base nitrogen in the ground state in comparison to light induced, cryo-trapped K- and M-states. A high M-state population could be achieved by preventing reprotonation of the Schiff base through a mutation of the primary proton donor (E108Q). Our data reveal unexpected large and alternating 13C chemical shift changes in the K-state propagating away from the Schiff base along the polyene chain. Furthermore, two different M-states have been observed reflecting the Schiff base reorientation after the de-protonation step. Our study provides novel insight into the photocycle of PR and also demonstrates the power of DNP-enhanced solid-state NMR to bridge the gap between functional and structural data and models.
PMID: 29027800 [PubMed - as supplied by publisher]
Visualizing Specific Cross-Protomer Interactions in the Homo-Oligomeric Membrane Protein Proteorhodopsin by Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR
Visualizing Specific Cross-Protomer Interactions in the Homo-Oligomeric Membrane Protein Proteorhodopsin by Dynamic-Nuclear-Polarization-Enhanced Solid-State NMR
Jakob Maciejko, Michaela Mehler, Jagdeep Kaur, Tobias Lieblein, Nina Morgner, Olivier Ouari, Paul Tordo, Johanna Becker-Baldus and Clemens Glaubitz
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b03606/20150713/images/medium/ja-2015-03606j_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b03606
...
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07-14-2015 02:59 AM
[NMR paper] Visualizing specific Cross-Protomer Interactions in the Homo-Oligomeric Membrane Protein Proteorhodopsin by DNP-enhanced Solid-state NMR.
Visualizing specific Cross-Protomer Interactions in the Homo-Oligomeric Membrane Protein Proteorhodopsin by DNP-enhanced Solid-state NMR.
Visualizing specific Cross-Protomer Interactions in the Homo-Oligomeric Membrane Protein Proteorhodopsin by DNP-enhanced Solid-state NMR.
J Am Chem Soc. 2015 Jun 23;
Authors: Maciejko J, Mehler M, Kaur J, Lieblein T, Morgner N, Ouari O, Tordo P, Becker-Baldus J, Glaubitz C
Abstract
Membrane proteins often form oligomeric complexes within the lipid bilayer but factors controlling their assembly...
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06-24-2015 01:08 PM
Proton-Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin
Proton-Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin
Meaghan E. Ward, Lichi Shi, Evelyn Lake, Sridevi Krishnamurthy, Howard Hutchins, Leonid S. Brown and Vladimir Ladizhansky
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja207137h/aop/images/medium/ja-2011-07137h_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja207137h
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/Vzwkh1cjxOU
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10-09-2011 06:15 AM
Proton Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin.
Proton Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin.
Proton Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin.
J Am Chem Soc. 2011 Sep 16;
Authors: Ward ME, Shi L, Lake EM, Krishnamurthy S, Hutchins H, Brown LS, Ladizhansky V
Abstract
We used high-resolution proton-detected multidimensional NMR to study the solvent-exposed parts of an integral seven-helical membrane proton pump proteorhodopsin...
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09-17-2011 08:21 PM
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR.
J Am Chem Soc. 2011 Mar 14;
Authors: Yang J, Aslimovska L, Glaubitz C
Environmental factors such as temperature, hydration, and lipid bilayer properties are tightly coupled to the dynamics of membrane proteins. So far, site-resolved data visualizing the protein's response to alterations in these factors are rare, and conclusions had to be drawn from dynamic data averaged over the whole protein...
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03-16-2011 04:15 PM
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR
Molecular Dynamics of Proteorhodopsin in Lipid Bilayers by Solid-State NMR
Jun Yang, Lubica Aslimovska and Clemens Glaubitz
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109766n/aop/images/medium/ja-2010-09766n_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/ja109766n
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/VmNlca5pCIw