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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

Nicole Pfleger

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
Online Publication Date Oct 30, 2007
Publication Date 2008-01
Deposit Date Nov 13, 2014
Publicly Available Date Mar 28, 2024
Journal Journal Of Biomolecular Nmr
Print ISSN 0925-2738
Electronic ISSN 1573-5001
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

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