Evidence map›Paper›PMID 30586409›Full record

ArticlePloS one2018

Raman spectroscopy of a near infrared absorbing proteorhodopsin: Similarities to the bacteriorhodopsin O photointermediate.

Gaoxiang Mei, Natalia Mamaeva, Srividya Ganapathy, Peng Wang, Willem J DeGrip, Kenneth J Rothschild

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.1field-weighted citation impact, top 26% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed, 13 citations in OpenAlex.

  1. Journal of chemical theory and computation · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Gaoxiang MeiMolecular Biophysics Laboratory, Photonics Center and Department of Physics, Boston University, Boston, Massachusetts, United States of America.ORCID 0000-0002-1244-5694
Natalia MamaevaMolecular Biophysics Laboratory, Photonics Center and Department of Physics, Boston University, Boston, Massachusetts, United States of America.
Srividya GanapathyDepartment of Biophysical Organic Chemistry, Leiden Institute of Chemistry, Leiden UniversityAR Leiden, The Netherlands.
Peng WangBruker Corporation, Billerica, MA, United States of America.
Willem J DeGripDepartment of Biophysical Organic Chemistry, Leiden Institute of Chemistry, Leiden UniversityAR Leiden, The Netherlands.
Kenneth J RothschildMolecular Biophysics Laboratory, Photonics Center and Department of Physics, Boston University, Boston, Massachusetts, United States of America.ORCID 0000-0002-2847-6671
Boston University · USLeiden University · NLBruker (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microbial rhodopsins have become an important tool in the field of optogenetics. However, effective in vivo optogenetics is in many cases severely limited due to the strong absorption and scattering of visible light by biological tissues. Recently, a combination of opsin site-directed mutagenesis and analog retinal substitution has produced variants of proteorhodopsin which absorb maximally in the near-infrared (NIR). In this study, UV-Visible-NIR absorption and resonance Raman spectroscopy were used to study the double mutant, D212N/F234S, of green absorbing proteorhodopsin (GPR) regenerated with MMAR, a retinal analog containing a methylamino modified β-ionone ring. Four distinct subcomponent absorption bands with peak maxima near 560, 620, 710 and 780 nm are detected with the NIR bands dominant at pH <7.3, and the visible bands dominant at pH 9.5. FT-Raman using 1064-nm excitation reveal two strong ethylenic bands at 1482 and 1498 cm-1 corresponding to the NIR subcomponent absorption bands based on an extended linear correlation between λmax and γC = C. This spectrum exhibits two intense bands in the fingerprint and HOOP mode regions that are highly characteristic of the O640 photointermediate from the light-adapted bacteriorhodopsin photocycle. In contrast, 532-nm excitation enhances the 560-nm component, which exhibits bands very similar to light-adapted bacteriorhodopsin and/or the acid-purple form of bacteriorhodopsin. Native GPR and its mutant D97N when regenerated with MMAR also exhibit similar absorption and Raman bands but with weaker contributions from the NIR absorbing components. Based on these results it is proposed that the NIR absorption in GPR-D212N/F234S with MMAR arises from an O-like chromophore, where the Schiff base counterion D97 is protonated and the MMAR adopts an all-trans configuration with a non-planar geometry due to twists in the conjugated polyene segment. This configuration is characterized by extensive charge delocalization, most likely involving nitrogens atoms in the MMAR chromophore.

Indexed as

BacteriorhodopsinsLightMutationOptogeneticsRetinaldehydeRhodopsins, MicrobialScattering, RadiationSpectrum Analysis, RamanStereoisomerismBacteriorhodopsinsproteorhodopsinRetinaldehydeRhodopsins, Microbial

Identifiers

PMID30586409
PMCPMC6306260
OpenAlexW2905663423

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.