Nicole Pfleger
Characterisation of Schiff base and chromophore in green proteorhodopsin by solid-state NMR
Pfleger, Nicole; Lorch, Mark; Woerner, Andreas C.; Shastri, Sarika; Glaubitz, Clemens
Authors
Professor Mark Lorch M.Lorch@hull.ac.uk
Professor of Public Engagement and Science Communication.
Andreas C. Woerner
Sarika Shastri
Clemens Glaubitz
Abstract
The proteorhodopsin family consists of hundreds of homologous retinal containing membrane proteins found in bacteria in the photic zone of the oceans. They are colour tuned to their environment and act as light-driven proton pumps with a potential energetic and regulatory function. Precise structural details are still unknown. Here, the green proteorhodopsin variant has been selected for a chemical shift analysis of retinal and Schiff base by solid-state NMR. Our data show that the chromophore exists in mainly all-trans configuration in the proteorhodopsin ground state. The optical absorption maximum together with retinal and Schiff base chemical shifts indicate a strong interaction network between chromophore and opsin. © Springer Science+Business Media B.V. 2007.
Citation
Pfleger, N., Lorch, M., Woerner, A. C., Shastri, S., & Glaubitz, C. (2008). Characterisation of Schiff base and chromophore in green proteorhodopsin by solid-state NMR. Journal of Biomolecular NMR, 40(1), 15-21. https://doi.org/10.1007/s10858-007-9203-5
Acceptance Date | Feb 1, 2007 |
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Online Publication Date | Oct 30, 2007 |
Publication Date | 2008-01 |
Deposit Date | Nov 13, 2014 |
Publicly Available Date | Nov 13, 2014 |
Journal | Journal Of Biomolecular Nmr |
Print ISSN | 0925-2738 |
Publisher | Springer Verlag |
Peer Reviewed | Peer Reviewed |
Volume | 40 |
Issue | 1 |
Pages | 15-21 |
DOI | https://doi.org/10.1007/s10858-007-9203-5 |
Keywords | Proteorhodopsin; Solid-state NMR; Schiff base; Retinal |
Public URL | https://hull-repository.worktribe.com/output/473025 |
Publisher URL | https://www.scopus.com/inward/record.uri?eid=2-s2.0-37849010835&doi=10.1007%2fs10858-007-9203-5&partnerID=40&md5=54a19424153e02f7c4007b51e2a8a204 |
Contract Date | Nov 13, 2014 |
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