Spectroscopic and photochemical analysis of proteorhodopsin variants from the surface of the Arctic Ocean

Proteorhodopsin (PR), a retinal‐containing seven transmembrane helix protein, functions as a light‐driven proton pump. Using PCR, we isolated 18 PR variants originating from the surface of the Arctic Ocean. Their absorption maxima were between 517 and 546 nm at pH 7. One of the isolates turned out t...

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Bibliographic Details
Published in:FEBS Letters
Main Authors: Jung, Jae Yong, Choi, Ah Reum, Lee, Yoo Kyung, Lee, Hong Kum, Jung, Kwang-Hwan
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2008
Subjects:
Arctic Ocean
Online Access:http://dx.doi.org/10.1016/j.febslet.2008.04.025
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1016%2Fj.febslet.2008.04.025
https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/j.febslet.2008.04.025
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Summary:Proteorhodopsin (PR), a retinal‐containing seven transmembrane helix protein, functions as a light‐driven proton pump. Using PCR, we isolated 18 PR variants originating from the surface of the Arctic Ocean. Their absorption maxima were between 517 and 546 nm at pH 7. One of the isolates turned out to be identical to GPR (green light‐absorbing proteorhodopsin) from Monterey Bay. Interestingly, 10 isolates had replaced a tyrosine in the retinal‐binding site (Tyr200 in GPR) with Asn. They showed a slower photocycle, more blue‐shifted absorption maxima at pH 10, and relatively larger Δ H and Δ S of activation of the transition between the O intermediate and the ground state compared to GPR.

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